To make use of protein-protein interaction network

The largest database of protein-protein interaction network has been laughed today, according to EurekAlert!, a science and technology news sharing platform of the American Association for the Advancement of Science (AAAS). The database is a collection of more than 62.55 million protein-protein interactions. Wit this data resource and recombinant proteins such as recombinant horse proteins, researchers can elucidate the effects of multiple genes on disease progression.

The importance of mapping large-scale protein-protein interaction network is widely recognized, but the data are scattered across a variety of academic articles. Researchers from the United States, Denmark and the United Kingdom collaborated and integrated more than 43,000 published articles from the data and created the database named InWeb_InBioMap.

"Modern genetic technology makes it possible to sequen- tally the genome of patients with cancer or mental illness on a regular basis, but understanding the cellular systems affected by the genetic genetic variation remains a major challenge," said team leader Dr. Kasper Raj. A more complete map of the physical interactions of human proteins will enable us to explore more precisely the cellular processes affected by the disease than ever before."

Li Taibo, a co-editor of the team, explains, "It is just like human society, proteins like to work in small groups. The social networking platform Facebook can infer people who might know each other, based on interaction patterns and interest sharing between networks, as well as between protein-protein interactions." By exploring possible pathways of protein-protein interactions, the genome and molecular pathways can be deduced, thereby deepening the understanding of life processes occurring in human cells. Clinicians can use this to look at patterns of genetic data and provide new molecular perspectives for finding new disease-causing genes.

The team is also continuing to develop other uses of the resource database, such as integrating proteomics, transcriptome and genomic data to improve understanding of complex biological systems, and the use of this information will help to understand cardiovascular disease, birth defects, cancer, reproductive disorders, mental illness and other pathogenic mechanisms. Flarebio offers superior recombinant proteins like recombinant CDH2 at competitive prices.

Whether the treatment of amyloid protein hypothesis loses the scientific basis?

Eli Lilly and Company recently announced the results of its Phase 3 clinical trial of Alzheimer's disease (AD) drug candidate, solanezumab. Although the results using recombinant mouse proteins are not satisfactory, this doesn't mean that the treatment of amyloid protein hypothesis lost the scientific basis.

Amyloid hypothesis began in the 1980s and is an important theory which has the most research evidence to support the interpretation of AD causes. AD is the most important form of Alzheimer's disease. The deposition of amyloid protein (β-Amyloid, Aβ) is one of the important markers of AD. Amyloid Hypothesis think that Aβ levels in AD patients are abnormally elevated due to imbalance between production and degradation, leading to the deposition of Aβ in the brain and leading to neuronal damage and death in the brain. It is the root cause of memory and cognitive decline.

Based on this theory, different therapies targeting Aβ have been developed. Some of them attempt to target Aβ-producing proteases to prevent Aβ production, while others hope to bind free Aβ monomers in the blood, preventing them from entering the brain to produce deposits. The current trial results show that these therapies are not yet effective in preventing cognitive decline.

"This may be related to the characteristics of some of the therapies," says Christian Haass, MD, head of the Munich-based Neurodegenerative Disease Research." For example, some drugs can only bind to Aβ monomers, but not to deposited Aβ fibers; In addition, drugs injected into the patient's body may bind to Aβ monomers in the bloodstream, resulting in insufficient drug to enter brain, reducing Aβ monomer in the brain."

Other drugs with different mechanisms are expected to bring about a turn for the better. Aducanumab, which can target Aβ deposition in the brain, is one of them. In early clinical trials, this antibody can eliminate Aβ deposition in the brain and reduce memory loss. Its Phase 3 clinical trial is expected to end in 2020. The researchers believe that the different modes of action of Aβ may be the key to alleviating symptoms.

In summary, the current clinical trials in the setbacks encountered in progress, but it does not necessarily explain the amyloid hypothesis is wrong. New drug development is a long and thorny road. We hope that the new drug development of AD can find the direction of progress and ultimately bring new treatment for patients. Flarebio provides good-quality recombinant proteins such as recombinant Itgb2 for your research.

To "starve" breast cancer cells to achieve treatment

How do cancer cells burn calories? New research from Thomas Jefferson University shows that breast cancer cells rely on different processes to convert fuel into energy. The results were recently published in the Journal of Biochemistry, which also publishes other studies on recombinant rat proteins.

Ubaldo Martinez-Outschoorn, M.D., an assistant professor of medical oncology at Thomas Jefferson University and a researcher at Jefferson's Sidney Kimmel Cancer Center, and his colleagues studied a protein that changes the metabolism of breast cancer cells. Protein TIGAR (an abbreviation of TP53-inducible glycolysis and apoptosis modulators) reduces the ability of cells to convert to sugars through the most common biochemical pathways and to generate energy through glycolysis. It is not clear how this metabolic change alters cancer cells or how cells acquire the energy needed to survive. Through a series of cell and mouse studies, researchers have shown that breast cancer cells with TIGAR proteins that are higher than normal abundance are more invasive and can grow faster than breast cancer cells with normal amounts of TIGAR.

Dr. Martinez-Outschoorn and colleagues showed that when cells express TIGAR, they exchange their metabolic pathways and rely on mitochondria for energy production. Interestingly, high levels of TIGAR produced by cancer cells also alter the metabolism of cells surrounding and maintaining breast cancer and have opposite metabolic effects. TIGARs don't increase their dependence on mitochondrial energy production, but rather make these supporting cells dependent on glycolysis and increased tumor growth. Previous studies have shown that glycolysis in tumors provides energy for cells, making breast cancer more aggressive.

"In fact, 70-80% of breast cancers show a high level of TIGAR, which provides new insights into our study," Dr. Martinez-Outschoorn said. "There are already treatments that block mitochondrial metabolism. We can make use of them to "starve" breast cancer cells."

The two drugs approved for other indications - metformin, antidiabetic therapy and doxycycline, antibiotics - are known to block mitochondrial metabolism. When researchers used these drugs to block TIGAR expression in breast cancer cells, they also blocked mitochondrial metabolism. And they saw a decrease in the aggressiveness of cancer.

"As these drugs have been approved, they have passed human safety tests. And if as our preliminary study shows that they do help to reduce tumor growth in patients, they can be used as a combination therapy with other drugs," said Martinez-Outschoorn.

To this end, Dr. Martinez-Outschoorn is working with Dr. Jennifer Johnson, MD, assistant professor of medical oncology, and Dr. Adam Berger, professor of surgery at Jefferson University, to conduct a clinical trial to test metformin for breast cancer, and women should take doxycycline before surgery. The study will collect and analyze patients' tumors to see if these drugs that inhibit mitochondrial metabolism may have an impact on tumor biology. Flarebio provides you with recombinant proteins of good quality such as recombinant CDH2.

The role of tau protein and phosphate in Alzheimer's disease

Alzheimer's disease is the most common form of dementia, and it is characterized by a gradual loss of cognitive ability, namely the ability to learn, memorize and plan. More than 35 million people worldwide are diagnosed with Alzheimer's disease. The figure continues to increase due to the aging population. Unfortunately, we have no way to cure this disease. The current treatment is effective, but it can only reduce the symptoms to a very low level. Therefore, understanding how Alzheimer's disease is formed and its hidden processes through recombinant human proteins is important for effective treatment of this disease.

Researchers have recently discovered a new and surprising clue about the role of tau and phosphate in Alzheimer's disease. The first evidence comes from genes. They unexpectedly found a gene that protects mice from Alzheimer's disease. The study also found that the protein formed by this gene will gradually decrease with the onset of Alzheimer's disease.

In conjunction with the use of cultured mouse neurons, the researchers carefully studied how this gene works and found that this gene affects the manner in which phosphate groups attach to tau proteins. This gene plays a protective role by establishing a special tau phosphorylation model.

The researchers also found that when mice were given a specific mode of attachment of phosphate groups, they were protected from Alzheimer's disease. The study changed our thinking about molecular events in Alzheimer's disease. Researchers have found that a specific tau phosphorylation pattern can prevent neuronal death in mice with this disease model. In other words, a phosphorylated tau that protects the brain from Alzheimer's disease can form in the brain. This challenges the conventional wisdom of researchers that tau phosphorylation only causes toxic effects and is "sinful" in the development of Alzheimer's disease. Flarebio provides you with good-quality recombinant proteins like recombinant Itgb2 at great prices.

AIDS is no longer the nightmare for a lot of people

Researchers have made significant progress in developing highly-potent vaccines for preventing HIV infection by use of recombinant horse proteins. For the first time, researchers have shown that a combination of using a common cold virus to induce vaccination with and injecting DNA-based vaccines allows the immune system to proactively protect the human intestine and body cavity from HIV infection.

The results of the study are published in the journal Nature's Scientific Report. The results of this study represent an important step in the first line of defense for the introduction of HIV at the site of infection.

Dr. Branka Grubor-Bauk, a senior author at the University of Adelaide and at the Basil-Hazel Institute for Translational Health, Queen Elizabeth Hospital, said, "Sexual activity is one of the main methods of HIV transmission, thus it is necessary to protect those parts of the body that are most likely to encounter a virus. A possible cause of previous unsuccessful trials of HIV vaccines was the lack of first line protection.

"In mice, we injected a rhinovirus (or common cold virus) into its nose, and the virus changed parts that included the HIV protein. At the same time, DNA-based vaccines were also injected to mouse skin, which produces a very specific response in the immune system," Dr. Grubor-Bauk said. "Importantly, the vaccine works in two different immune systems: white blood cells which attack the HIV virus and specific antibodies which recognize and shut down HIV-positive cells."

Eric Gowans was responsible for the study, and he also worked in the surgical department at a university in the Basil Hetzel Institute. "HIV has the Tat effect, and one of the advantages of our vaccine approach is that antibodies can keep the Tat effect and prevent the propagation of the HIV virus," Gowans said.

"Overall, we found a significant reduction in the number of HIV-infected mice in our study. Our results now support further testing against HIV vaccines," he said. Flarebio offers recombinant proteins of good quality like recombinant CDH15 at great prices.

To treat lung cancer spread in another way

Scientists at the University of New York and the University of Texas have found through recombinant rat proteins that one component of a cancer cell, which acts like a cellular post office, may be the key to preventing lung cancer from spreading to other parts of the body. This finding can point to new therapies that target a specific communication mechanism in the cell. This communication triggers a change in the perimeter of the cell scaffold. It changes from a fixed shape to an organ that has a more unstable shape which can move freely within the body.

"Cell post offices", or the Golgi apparatus which are more well-known, are able to transport proteins to other parts of the cell or transport them outside the cell. The researchers found that a protein called PAQR11, inside the cell postoffice, from another protein called Zeb1, receives a signal that the two proteins communicate between the Golgi membrane and transport the membrane. These membrane bags, or vesicles, alter their route of delivery, altering the perimeter of the cancer cells to detach the cells from their fixed position in the lungs and freeing them to other parts of the body.

"If we think of a cancer cell as a tent structure, it has fixed edges to keep its shape and hold it in order to retain its contents. It can't move except its change in structure," says Dr. Daniel Ungar of the Department of Biology at New York University.

"To move the tent, we have to rearrange its contents to destroy its edge and move it away from the fixed position. There is a similar process when the cancer metastasis happens, and its outer edge changes so that it can't be fixed."

Golgi, the communication center between proteins, hencing the name "cell post office", receives a communication signal between two proteins that signal the movement of the membrane around the cell that should be changed. This movement changes the circumference of cancer cells just like the edge of a tent is destroyed to make them free from original resting place to anywhere of the whole body.

"Since we recognize this system, it is possible to develop a drug that interferes with this communication and prevents the Golgi apparatus from promoting the movement of the membrane bag. The next phase of this study will look at how we can work without interfering normal cellular function under the premise of targeting this process," Dr. Ungar added.

The study, funded by the National Institutes of Health, the American Cancer Society and the Texas Cancer Prevention Institute, was published in the Journal of Clinical Research. Flarebio provides you with good-quality recombinant proteins such as recombinant PIGR at competitive prices.

A mysterious sheath-like structure occupies 47% of the part of each chromosome

Chromosomes contain not only more than 25,000 genes. Scientists found that a mysterious sheath-like structure occupies 47% of the part of each chromosome through recombinant mouse proteins. After modeling the length, width, surface area, volume, and DNA density of all normal human chromosomes, researchers found something important to our understanding of the internal structure of the chromosome. "Defining all 46 chromosomes in humans forces us to reconsider the idea that chromosomes are composed almost entirely of chromatin," said biologist Daniel Booth. "This assumption has never been challenged in 100 years." In their analysis, Chromatin accounts for only 53 to 70 percent of all chromosomal components.

Another structure, called the periphery of chromosomes, accounts for 30 to 47 percent of chromosomes, which researchers have observed in the past but don't know how much they are. This means that for any chromosome, DNA and its supporting protein may account for only half of all components. "The first application of 3D-CLEM analysis has produced a remarkable and surprising conclusion that a large part of the total volume of the mitotic chromosome is not composed of chromatin, but rather consists of the periphery of the chromosome," they wrote in the paper.

At this stage, people still don't understand what the specific function of this structure is, but the researchers suspected that its function may be some kinds of "sheath" so that chromosomes are separated from each other in cell division. This has also been supported by previous studies that have shown that this structure is partly due to the Ki-67 protein. Ki-67 is a marker of cell proliferation and binds to the chromosomal surface to isolate sister chromatids. If this is really the function of the chromosomal sheath, it means that this structure plays an important role in preventing the occurrence of an error in cell division.

In addition to its function, there are many things we don't know about this mysterious structure. We don't know whether it works as a liquid or solid film and how it affects the structural changes of chromatin during cell division. Therefore, it appears to be returning to the most basic cellular makeup problem.

"Now we have to rethink how chromosomes are constructed and how they are separated when they divide, because they are covered by other materials," said research team member Bill Earnshaw. This research paper has been published in the journal Molecular Cell. Flarebio provides you with superior recombinant proteins like recombinant PIGR at competitive prices.

The mechanism of cancer tumor cells becoming cancer stem cells that can sustain long-term growth

International research, led by scientists from the London Creek Institute and the Hebrew University of Jerusalem, sheds light on the survival mechanisms in cancer cells that can re-emerge even after aggressive treatment. In a paper published in Science which also publishes some other studies on recombinant human proteins, the researchers describe the mechanism by which cancerous tumor cells become cancer stem cells that can sustain long-term growth.

When cancer develops, the resulting cells are heterogeneous in their biological properties and have different contributions to tumor development. Only a small percentage of cancer cells can form new tumors or metastases, and these are called "cancer stem cells". This difference between tumor cells constitutes a major challenge in understanding the nature of the tumor, its sensitivity to drugs and the effective treatment of all tumor cells.

"Many chemotherapeutic agents leave a small amount of cancer stem cells, causing disease to re-emerge after a few years," said Eran Meshorer, director of the Stem Cell and Epigenetics Laboratory of the Life Sciences Institute. "Therefore, it is important to identify cancer stem cells and characterize the differences between different tumor cells as a basis for detection of weaknesses during disease progression."

Cancer stem cells are not limited to the tumor itself. They can re-engage in a healthy environment and stimulate the disease. In order to study the characteristics of these unique cells, Prof. Dr. Meshorer and Dr. Alva Biran from the Hebrew University collaborated with Dr. Paula Scaffidi and Dr. Christina Morales Torres from the Crick Institute in London. The international team also includes Dr. Ayelet Hashahar Cohen of the Hebrew University, Dr. Rotem Ben-Hamo and Sol Efroni of Bar-Ilan University and Dr Tom Misteli of the NIH National Cancer Institute.



The team found that in many cancer types, those cancer stem cells lost one of their DNA packaging proteins, H1.0. By binding to DNA, the H1.0 gene was expressed.

"In order to understand the mechanism of action, we mapped the interaction pattern with DNA and found that it binds to the regulatory region of the gene," explained Professor Meshorer. "When the levels of H1.0 increase, these genes can inhibit the proliferation of cancer cells."

The study is based on epigenetics - a scientific field that investigates gene expression by switching the DNA on and off genes. To identify cancer stem cells from other cells in the tumor, the team studied the epigenetic mechanisms that differentiate at least sorted cells with infinite splitting properties and the potential to produce growth, as well as more sorted cells lacking this ability.

The results show an inverse relationship between H1.0 and cancer cell division: with the decrease of H1.0 levels, the greater the potential for uncontrolled division of the cells is. In contrast, high levels of protein prevent this process. We found that the disappearance of H1.0 protein is the characteristic of cancer stem cells, and it is necessary to maintain the ability to divide and the potential for growth.



This finding opens the door to medical intervention for cancer stem cells, aimed at restoring high levels of H1.0 in all cancer cells and blocking the differentiation of cancer cells. Although further research is needed to understand the usefulness of H1.0 protein in preventing cancer growth and spread, this study significantly expresses the cancer stem cell mechanism and relatively new epigenetic approaches to cancer research. Flarebio offers recombinant proteins of good quality such as recombinant Cd44 at good prices.

Scientists find new method of treating metastatic lung cancer

The rapid spread of lung cancer cells in the body makes it difficult to treat lung cancer. However, according to a new study using recombinant mouse proteins and led by scientists in California, the metastasis ability of cancer is likely to be due to inactivation of a single protective protein in tumor cells. The study found that the gene of a protective protein (CIC) in lung cancer patients had some frequency mutations which make lung cancer cells easy to transfer to other parts of the body.

In addition, the researchers have determined that the inactivation of this protein makes lung cancer cells have abnormal biochemical changes. Even if there is no mutation in the CIC gene itself, some of these abnormalities will drive the growth of the tumor.

Senior researcher Dr. Trever Bivona recently pointed out that restarting CIC may be able to prevent the spread of lung cancer. "We found that this protein was first identified as a regulator of Drosophila development and is known to directly control the normal development of the balloon in the lung and can be inactivated to cause cancer spread. Although it is already possible to re-activate CIC, more work is needed to reveal the validity of such a strategy."

The study was conducted by scientists from several research institutions, focusing on the most common lung cancer - non-small cell lung cancer. They directly inoculated fluorescently labeled human lung cancer cells into specific parts of the lungs that mimic the disease and used gene sequencing to measure data from three closely-related human lung cancer cell lines. This work quickly led to the CIC gene deletion and the corresponding lung metastasis phenomenon.

The researchers then analyzed genetic data from hundreds of human lung cancers and found that the percentage of CIC mutations in metastatic lung cancer increased six-fold compared with those who had lung cancer spread. The researchers also determined that even if the CIC gene is normal, CIC protein activity may also be inhibited in some metastatic lung cancer. They found that MAPK signaling pathway often makes CIC protein inactivation.

Whether the mutation is caused by genetic factors or by the MAPK pathway disorders, decreased CIC activity caused a series of adverse consequences. Drugs that block hyperactivated MAPK signaling, known as RAF-MEK-MAPK inhibitors, have been used to counteract overgrowth of tumors. New findings suggest that these drugs may also prevent the spread of cancer by preventing the inactivation of CIC. Flarebio provides you with good-quality recombinant proteins such as recombinant TLR2 at good prices.

The role of a protein crucial for melanoma cell survival

The main objectives of the Spanish National Cancer Research Center (CNIO) Melanoma Task Force are to identify biomarkers of tumor progression and to validate new targets for melanoma treatment. Their research is particularly focused on finding "fingerprint" features of melanoma that distinguish this type of cancer from other types of cancer. A new study in the field, published in Nature Communications which also publishes other studies on recombinant human proteins, describes the role of a protein crucial for melanoma cell survival (CPEB4).

Melanomas are particularly aggressive, and the mechanism by which such behavior is driven is found to be difficult due to the high rate of unexpected mutations associated with the malignancy. The melanoma team, led by Marisol Soengas, is not only a senior author of this article, but also an expert on the "identity" of melanoma.

"In previous studies, we have shown that melanoma is very different from other types of tumors, because melanoma can activate autodegradable (autophagy) mechanisms. For example, it can control the internalization and secretion of molecules," Soengas explains. The CPEB4 protein of broad interest in the cancer field plays a selective role in melanoma cells and is indispensable.

Broadly speaking, CPEBs are involved in the regulation of gene expression and are associated with important cellular processes such as cell division, cell differentiation, cell polarization and cell migration. In a variety of tumor cells, CPEBs expression levels vary and look on the contrary, and they sometimes promote tumor and sometimes are anti-tumor. These effects have been described in other types of tumors, but not in melanomas.

CPEB4 is also a member of this family, which is "particularly attractive" to the authors because of its overexpression in tumors, such as with invasive gliomas and pancreatic cancers. As they pointed out, the level of this protein is very high in the early stages of melanoma, which makes the researchers suspect that it is related to cell proliferation, while they do not know the extent of this association.

Soengas' team compared the effects of CEPB4 on various tumors and noted that melanoma cells are "more dependent on this protein", because inhibition of CEPB4 can greatly inhibit melanoma cell proliferation. This "addiction" makes melanoma more vulnerable to attacks against this pathway of drugs, so CEPB4 can be a new target for the treatment of melanoma.

The researchers also said that CPEB4 and melanoma are closely related, because the protein can regulate factors (such as melanoma cells have unique functions MITF and RAB27A) expression. "Thus, CPEB4 may be a primary factor in distinguishing between the intrinsic characteristics of melanoma and other diseases," Soengas concluded. Flarebio offers good-quality recombinant proteins like recombinant TLR2 at competitive prices.

Scientists develop new way of diagnosing diseases

Maybe you never thought that music and genes can be linked together, but the combination of the two may be able to change the medical diagnosis in the future. Music and genes are repetitive, and the number of choices is limited. A gene has 4 base pairs, and music has 12 kinds of notes. This logic is used to transform protein structures into melodies so that they are no longer passed through the eyes but analyzed with the ears. Researchers who put this idea say that their melodies can be used to teach protein science and can be used to determine mutations in the near future.

Researchers at the University of Tampere in Finland, the University of East Washington and the Francis Crick Institute in London, England, conducted research using recombinant horse proteins and believed that their technology can help scientists more easily identify abnormalities in proteins. "We believe that in the future, people will eventually hear the data and extract important information from it," says Jonathan Middleton, Ph.D. of the University of East Washington. "The ear may detect more information than the eye. If the ear can do that, then you can liberate your eyes and pay more attention to other things."

Proteins have many different functions, and they are usually studied through observation under the microscope with the eyes. Now, researchers use an "audible" technique to convert protein data information into melodies. The study, published in the journal Heliyon, aims to answer three main questions: What does the data sound like? Are there any benefits? Can we hear the anomaly from the data?

An introductory excerpt shows the melody of the 1r75 protein. Researchers hope that someday other molecules can also be converted to melodies or they can even "listen" to the complete genome. This melody was created by the combination of Dr. Middleton's compositional techniques and algorithms so that other people could use a similar process to write melodies for proteins. When people hear these melodies, a large number of people can recognize the connection between tone and vision (such as images and tables), which means "listening" proteins are simpler than imagined. According to them, these melodies sound wonderful, which can also encourage scientists to listen several times to more accurately analyze the protein. The protein data information is converted to melody using an "audible" technique.

"Protein folding is one of the most annoying parts of the molecular biology field," says Dr. Robert Bywater of the Francis Crick Institute. "Researchers need to identify not only the type of folding but also the clues to its many functions." Information is not easy, and music acts as a power to achieve the release of this information.

Researchers say their melodies can be used to teach protein science and to determine mutations in the near future. But its application is not limited to proteins. Researchers hope that in the future one day other molecules can also be converted to music and "audible" technique even can be used to listen to the entire genome. This multidisciplinary approach (combining genetics and music) provides a new perspective on the complex issues of biology. If you’re do related research, recombinant proteins including recombinant Itgb1 from Flarebio will be good choices for you.

New therapeutic target of type 2 diabetes: decomposition of branched chain amino acid

A study published today in the Journal of the Public Library of Science has identified five genetic variations associated with higher levels of the branched-chain amino acids isoleucine, leucine and valine. Through research using recombinant rat proteins, the researchers also found that these gene mutations are associated with an increased risk of type 2 diabetes.

A team led by the Department of Epidemiology at the University of Cambridge Medical Research Council (MRC) made use of large-scale genetic data and detailed measurements of branched-chain amino acids and their metabolites in more than 16,000 volunteers.

Branched chain amino acids play a fundamental role in human metabolism, and it is the basis of protein. Unlike the other 20 amino acids, they can't be produced by the human body. This means that their level depends entirely on external resources (food sources or dietary supplements) and the body's metabolic capacity.

Up to now, although higher circulating levels of branched-chain amino acids have been found to be associated with type 2 diabetes, no study has been able to determine whether the association is causal. This is important because if found to be causally related, dietary intake reductions or changes in the metabolism of these amino acids may help to prevent the growing prevalence of diabetes and the severity of the disease.

Researchers studied more than 10 million genetic variations in more than 16,000 men and women and found genetic differences in five human genomic regions associated with higher levels of circulating branched-chain amino acids. They then found that in 300,000 people, including 40,000 people with diabetes, those with genetic differences associated with higher levels of branched-chain amino acids were at higher risk of developing type 2 diabetes, providing strong evidence of causality.

The PPM1K gene has been found to have the strongest association with all three amino acid levels and a higher risk of developing diabetes, and can encode a known regulator that plays a pivotal role in the breakdown of branched-chain amino acids. This suggests that impaired decomposition of these amino acids may make individuals at higher risk of developing type 2 diabetes. Intervention on this pathway may reduce the risk of diabetes.

"Our results suggest that therapeutic strategies for the metabolism of branched-chain amino acids can help to reduce the risk of diabetes, which we already know about," said Claudia Langenberg, MD from the MRC Epidemiology Unit at the University of Cambridge. Clinical trials are now needed to determine whether drugs that break down on branched-chain amino acids can reduce the risk of type 2 diabetes. Flarebio provides superior recombinant proteins like recombinant ITGB1 at great prices.

The preservation of β-keratin and pigment bodies in the fossil

Chinese and American scholars completed an article entitled "Early Cretaceous birds - the beginning of the Confucius bird feather keratin and molecular evidence of pigment body and published the paper on November 22 online in the Proceedings of the National Academy of Sciences, which also has other studies on recombinant horse proteins.

Dr. Pan Yanhong at Nanjing institute of geological paleontology, Chinese academy of sciences, Academician Zhou Zhonghe at Institute of Palaeontology and Paleoanthropology, Chinese Academy of Sciences, Professor Zheng Xiaoting from Linyi University, Shandong Province, China Prof. Shi Weicai from North Carolina State University, USA and his team conducted detailed Ultrastructure and biochemical analysis on the plumage of the first Confucius fossil specimen in the Shandong Tianyu Nature museum, confirming the preservation of β-keratin and pigment bodies in the fossil of 130 million years ago for the first time.

Current birds have colorful colors, which mainly depends on the feathers with the pigment body and feather internal structure. Feather pigment particles can be formed with the feathers into the different parts of the feathers, and thus the internal structure and other factors with the feathers can determine the different colors of the feathers.

However, the previous analysis of fossil feather pigments failed to accurately complete pigmentation of the signal in situ calibration to the pigment body. In this paper, a variety of chemical and molecular techniques were used to analyze chemical signals, including the immunoelectron microscopy (SEM) and ultra-high-resolution elemental energy spectroscopy (EHR), which were applied to fossil analysis for the first time. Their results not only confirmed the preservation of β-keratin in the fossils of 130 million years ago, but also confirmed that the micro-structure of feather fossils is wrapped by β-keratin, which are indeed the chromosomes of feathers. This work has advanced the age of β-keratin preservation for at least 50 million years, which is of great significance to better understand the soft tissue structure, the preservation of fossil molecules and the evolution of feather ultrastructure in ancient fossils. Flarebio provides you with superior recombinant proteins including recombinant Cdh11.

A protein that plays an important role in the accumulation of LDL cholesterol

The team led by Yale University has identified a protein that plays an important role in the accumulation of LDL cholesterol in blood vessels. The research was conducted using recombinant rat proteins. "This finding could lead to a treatment strategy that blocks LDL accumulation, which can help to prevent or slow the arterial blockage that causes heart disease," the researchers said. The study was published in the November 21 issue of Nature Communications.

When certain proteins (called lipoproteins) in the body bind to fat in the blood and transport the fat to the cells, the animals' blood vessels are blocked by fat and cholesterol. Scientists at first thought that LDL receptor molecules are responsible for intracellular LDL transport. However, in view of the fact that some individuals lack LDL receptors still have high levels of LDL, so questions remain about the mechanism.

To identify the mechanism, the team screened more than 18,000 genes (from the inner layers of human blood vessels) from the endothelium. They examined the genes involved in the process of LDL transfer into endothelial cells. The researchers found that the protein called ALK1 contributes to the pathway of LDL entry into the cell. "We have shown that ALK1 binds directly to LDL," said senior author William Cessa and professor of pharmacology Alfred Gilman. The team also identified the "LDL-ALK1 pathway" that helps LDL transit from the bloodstream to the tissues.

"The role of ALK1 in LDL accumulation has not been previously known, and the discovery of ALK1 as an LDL-binding protein suggests that it may initiate early stages of atherosclerosis. If we can find a small molecule or antibody that prevents ALK1 approach, then it can be used in conjunction with lipid-lowering strategies."

Current lipid-lowering strategies include statins, and it targets LDL cholesterol levels in the blood. "Therapeutic agents that block ALK1 will be a unique strategy to reduce the burden of atherosclerosis and have synergistic effects with lipid-lowering therapies," Sessa said. Heart disease caused by vascular damage is the leading cause of death worldwide. Flarebio provides you with good-quality recombinant proteins like recombinant Cdh26 at good prices.

Overweight can lead to abnormal blood flow, resulting in multiple myeloma

A new study from the University of Washington's St. Louis School of Medicine shows that overweight can lead to abnormal blood flow and may lead to multiple myeloma. We know that overweight or obesity increases the risk of multiple myeloma, a plasma cell tumor that occurs in the blood and bone marrow, and that the disease occurs more often after the age of 60. Before the occurrence of multiple myeloma, patients often appear first known as MGUS blood abnormalities. This anomaly refers to that the plasma cells will produce a number of antibody proteins, and this pre-cancerous lesion generally shows no symptoms, so it is difficult to be diagnosed.

"Our study using recombinant human proteins found that obesity can be a risk factor for predicting multiple myeloma," said Dr. Su-Hsin Chang of the University of Washington. "If a patient is diagnosed with MGUS, normal body weight is likely to be a preventable development method of multiple myeloma."

The researchers analyzed data from 7,878 patients (mainly males) who were diagnosed with MGUS between October 1999 and December 2009, and these data were obtained from the American Legionnaire database. Among these subjects, 39.8% were overweight and 33.8% were obese. The researchers followed the group to see if they eventually developed multiple myeloma. Finally, the researchers found that 4.6% of overweight patients (the average follow-up time of about 5.75 years) and 4.3% of obese patients (average follow-up time of about 5.9 years) eventually developed into multiple myeloma, and normal weight patients were only 3.5 %. For multiple myeloma, the results were statistically different. Overweight MGUS patients and obese MGUS patients were 55% and 98% more than normal-weight patients to be likely to develop multiple myeloma.

MGUS patients have elevated levels of antibody M (IgM), while about 3% of people who were more than 50 would show IgM rise, so MGUS is difficult to diagnose and there is no very effective treatment. Multiple myeloma is the third largest blood tumor. According to the American Cancer Society, in 2016, it is expected to have 30330 new patients, and about 12650 patients will die of multiple myeloma.

Dr. Su-Hsin Chang saidm, "According to our findings, overweight and obesity are risk factors for MGUS development into multiple myeloma, and our overweight and obesity are human intervention. We hope that our research results will provide a new strategy for the treatment of our disease. Moreover, we will further study the mechanism of obesity in promoting the development of MGUS to multiple myeloma." Flarebio provides you with good-quality recombinant CDH2 at great prices.

APOL1 gene can induce kidney disease

According to an article published in the November 18 issue of the American Journal of Nephrology, the National Institutes of Health System for Children has discovered a gene, APOL1, which induces kidney disease. The new form of the mutated APOL1 gene increases the risk of chronic kidney disease among people of African descent. Using a powerful genetic approach and recombinant horse proteins, national researcher of children was able to mimic APOL1 in Drosophila renal cell pathology. It opens the door to identifying other proteins that interact with APOL1, which is an important first step in identifying kidney disease that is currently drug-free.

The advantages of Drosophila in biomedical research include its rapid generation time and unparalleled ability to explore the basic biological processes of human underlying diseases through rich, complex genetic tools. People of African descent usually inherit APOL1 mutant genes to protect Africans from sleeping sickness in Africa, but this gene increases the odds of developing certain types of kidney disease by 17 to 30 times or more. Individuals are at higher risk of being infected with human immunodeficiency Viruses (HIV). Drosophila kidney cells, called kidney cells, accurately mimic the pathological features of human kidney cells in APOL1-associated kidney disease.

"Kidney cells have striking structural and functional similarities to mammalian podocytes and proximal tubule cells," says Zhe Han, an advanced Drosophila expert and associate professor of cancer and immunology at the Center for Cancer and Immunology. "This provides us with a simple kidney disease model system."

In a recent study, Han's team cloned the mutated APOL1 gene in cells from podocytes cultured in patients with HIV-associated nephropathy. They created transgenic Drosophila, similar to human APOL1 kidney cells, and observed that the initial transgene caused an increase in cellular functional activity. However, as the flies age, APOL1 leads to decreased cell function, increased cell size, abnormal vesicular acidification and accelerated cell death.

"The main function of kidney cells is to filter proteins, remove toxins from flowing blood, reabsorb protein components and chelate harmful toxins. Surprisingly, these cells begin to become more active and play a temporary role at a higher level. The cells become bigger and stronger, but they can't sustain this enhancement," said Han. "Cells die and cell hypertrophy is the way the human heart responds to stress overload after swelling to twice its normal size. We think that kidney cells may use the same coping mechanism."

The Children's Research Group is a multidisciplinary team of members from the Cancer and Immunology Research Center, the Center for Genetic Medicine Research and the Department of Nephrology. The group also characterizes flies phenotypes associated with APOL1 gene expression, which will facilitate the design and implementation of Drosophila gene screening methods to identify proteins that interact with APOL1 and contribute to disease mechanisms. Such proteins represent potential therapeutic targeting targets. Transplantation is currently the only option for patients with kidney disease associated with APOL1.

"It's just the beginning," Han said. "Now that we have an ideal preclinical model, we plan to start testing out-of-the-box therapeutic compounds, such as different kinase inhibitors, to determine if they block any steps leading to kidney cell disease." Flarebio offers recombinant proteins such as recombinant Itgb2 at competitive prices.

BAG5 protein can save the function of anti-oncoprotein p53

According to research using recombinant dog proteins, among the anti-oncoproteins found so far, p53 is undoubtedly one of the most well-known. It can achieve the curative effect of cancer by affecting cell division, apoptosis, metabolism and other important processes. In nearly half of the tumors, the gene TP53 which expresses this transcription factor show mutations, making p53 lose anti-cancer function. And some functional (GOF) mutations may even make p53 directly "renegade" and promote canceration and tumor resistance.

Mutant p53 is characterized by a greater stability, reflected by being more difficult to be mediated and degradated by ubiquitin ligase MDM2 and CHIP. Interestingly, this stability is limited to cancer cells but not in the normal cells. This allows the mutant p53 to accumulate in the tumor to a high level so as to play its role in promoting cancer. Then, what kind of difference do cancer cells have to make mutant p53 to accumulate at a high level?

Recently, the research team of Prof. Wenwei Hu and Prof. Zhaohui Feng of Rutgers, The State University of New Jersey found that BAG-2-related anti-apoptotic gene (BAG) family proteins BAG5 and BAG2 can prevent pan- Ligase and mutant p53 binding, thereby giving the latter cell-specific stability in the cancer. The results are published in the recent Nature Publishing Group publication Cell Discovery.

In a variety of human breast cancer and lung cancer cell lines and other systems, BAG5 of the five BAG domain can be R175H, R248W or R273H mutant p53 DNA binding domain (DBD) interaction, and BAG5 and wild type P53 between no affinity. At the same time, BAG2, another member of the BAG family, was found to have synergistic effects with BAG5 in enhancing mutant p53 stability. Concomitantly, when BAG5 was overexpressed, the level of mutant p53 was increased in cancer cells, and it decreased when BAG5 was knocked down.

By this interaction, BAG5 prevents MDM2 and CHIP from modifying ubiquitination of mutant p53, thereby ultimately inhibiting degradation of the p53 by the proteasome. Further experiments have shown that BAG5 is essential for the development of functional R248W mutations to play a role in carcinogenesis, including the ability to promote proliferation, proliferation, and drug resistance in cancer cells. It is worth noting that BAG5 is overexpressed in a variety of tumors including breast cancer, skin cancer, colorectal cancer, lung cancer and so on. And the higher the expression level, the worse the prognosis of patients.

BAG family proteins play an important regulatory role in cell division, differentiation and apoptosis, and their common BAG domains have molecular chaperone activity. In this study, BAG5 was found to have proto-oncogenic properties that enhance the ability of cancer cells to proliferate, diffuse and resist drug resistance by increasing the level of functional mutant p53 protein. Therefore, BAG5 has a potential as a therapeutic target for tumors expressing the aforementioned p53 protein. Flarebio provides good-quality recombinant proteins such as recombinant CDH2.

It's promising to treat Alzheimer's disease using gene therapy

Recently, a study from the Imperial College of Technology in London, England, has provided new possibilities for the treatment of Alzheimer's disease through recombinant human proteins. The researchers said their mice experiments showed that gene therapy may be successful in the treatment of Alzheimer's disease. The study was published in the Proceedings of the National Academy of Sciences.

Researcher Magdalena Sasite participating in the study of Imperial College London said that they used the modified lentiviral vector to inject a gene called PGC1-α into the memory region of the mouse brain. These mice just began to develop early symptoms of Alzheimer's disease. The results showed that this therapy prevented the accumulation of β-amyloid in the brain of mice, which is thought to cause brain cell death and was closely related to the pathogenesis of Alzheimer's disease.

The researchers said that after treatment with gene therapy for 4 months, few amyloid plaques of Alzheimer's disease existed in these mice brain. In the task-testing of memory, these treated mice behaved as well as healthy mice. In addition, their brain memory region also showed no loss of brain cells.

Genetic factors play an important role in the pathogenesis of Alzheimer's disease. Preston Estepp, director of Gerontology Research of "Personal Genome Project" of Harvard University School of Medicine and the author of the book Longevity of the Gene, said, "There are two most significant genes. They are apolipoprotein E (APOE) and amyloid precursor protein (APP)."

"More and more research evidence suggests that APOE is responsible for transporting iron into the brain. With the increase in iron accumulation, APP protein is also increasing to protect the brain cells and tissues. Then, the special cells that function as cleaners begin to work. A small portion of the APP will be cut off and discarded, and the abandoned part is β-amyloid protein, which is the culprit of formation of brain age spots. The enzymes which play cutting role play other roles in the cells, but the APP cut on the human body does not make any sense and may even cause collateral damage to the human body. With the accumulation of β-amyloid, functional brain cells will be killed and replaced," Estepp made the above explanation for the interaction of APOE and APP genes with iron.

Estepp suggested that we should pay more attention to the iron content of food. "For normal women, 18mg of iron can provide them with 100% of the daily intake. For other adults, the general daily 8mg of iron can be met," Estepp also said, "There are individual differences in iron uptake efficiency. In addition to the iron content of the food and the reasonable control of the intake, we can also monitor the key biomarkers for iron, including serum iron, serum ferritin, hemoglobin and so on.” Flarebio offers recombinant proteins of good quality such as recombinant Itgb2 at great prices.

There may be a short course of treatment for chronic hepatitis C

Recently, the study report of the annual meeting of the American Association for the Study of Liver Diseases states that RG-101, a candidate drug from Regulus Therapeutics in combination with direct-acting antiviral (DAA) therapy requires only four weeks of treatment to cure most of the hepatitis C patients, according to the research through recombinant rat proteins.

The treatment of hepatitis C in recent years has undergone great changes with the introduction of DAA therapy. This type of drug works directly on targets associated with hepatitis C virus replication. Compared with previous interferon-based therapies, it has better efficacy and fewer side effects. The advent of DAA drugs has made it possible to cure hepatitis C, but the current standard course of oral DAA is 8 to 24 weeks. The shortest course of treatment will not be less than 8 weeks.

RG-101 is an innovative injection therapy targeting microRNA-122 (miR-122, miR-122) developed by Regulus. MiR-122 is one of the most abundant miRs in the liver and plays an important role in the stability, replication and protein translation of hepatitis C virus in hepatocytes. The advantage of RG-101 is that it targets hepatitis C virus in a completely new pattern, and it is effective against all genotypes of hepatitis C virus against strains that are resistant to certain DAA drugs because of gene mutations. Therefore, its combination with DAA therapy may enhance the efficacy of hepatitis C virus and shorten the course of treatment.

The results reported in this scientific report came from a clinical phase 2 trial involving 79 patients with HCV. These patients received RG-101 injections on the first day and were divided into three groups, receiving four weeks of different types of oral DAA therapy approved by the FDA. The first group received ledipasvir / sofobuvivr treatment; the second group received simeprevir treatment; the third group received daclatasivr treatment. At the end of the 28-day course, the patient received another RG-101 injection on day 29.

The results showed that at the 12th week after the end of the treatment period, 100% of the patients in the first group, 96% in the second group and 92% of the third group had decreased to undetectable levels. At week 24 after the end of the treatment period, 100% of the patients in the first group, 80% of the patients in the second group and 89% of the patients in the third group were undetectable. And these combination therapies only have mild to moderate side effects, and no patients stopped treatment due to side effects.

"The focus of this research is to find shorter, better-effective and safer methods of treatment for hepatitis C," said one of the head of the clinical trial at the Hepatology Center of Buda in Budapest, Hungary. "Our results suggest that there may be a short course of treatment for chronic hepatitis C," Dr. Mihály Makara said. Flarebio provides you with good-quality recombinant proteins such as recombinant CDH15 at great prices.

Science: Amyloid protein lesion also can be the bane of tumor

Scientists at the Flanders Institute for Biotechnology (FIB) in Belgium have published a study releasing a patent called Pept-in in the world-renowned scientific journal Science. This patent was developed through recombinant human proteins and can simulate Alzheimer's disease Amyloid formation mechanism and make use of amyloid polymerization properties to make the disease protein of tumor and other diseases assemble and lose function, thus achieving therapeutic purposes. This represents a new idea of drug development and may be able to bring targeted new treatment of a variety of diseases including cancer.

Amyloid protein is a ubiquitous protein found in our daily foods, such as boiled eggs and beer foams. It has also been shown to be associated with Alzheimer's disease, multiple sclerosis, Parkinson's disease, glaucoma and other diseases. In particular, a typical pathological change of Alzheimer's disease is amyloidogenic amyloidosis in the brain to form amyloid plaques. With regard to amyloidosis related to medical research and drug development, the current mainstream idea is to inhibit the protein to treat diseases, rather than the use of this protein. There has been a significant capital injection into the development of new drugs that target amyloidogenic targets such as beta amyloidosis and Tau protein.

Amyloid formation seems to imply a negative pathogenic signal. However, research teams led by Prof. Frederic Rousseau and Professor Joost Schymkowitz of the VIB Institute have used these substances to form tumors and attack many diseases.

They used their own development of Pept-in patented technology to design and synthesize a vascin called amyloidogenic material (a characteristic amyloid protein structure of short-chain peptide sequence). The molecule has to promote amyloidosis which can rapidly penetrate the tumor cell membrane and promote the tumor cells on the vascular endothelial growth factor receptor 2 (VEGFR2) protein cohesive degeneration and lose their function. VEGFR2 is an important molecule to promote the survival of tumor growth. It means that the inactivation of cancer can inhibit the therapeutic effect.

"This method allows the surface protein of the tumor to condense. It is just like a tumor-like spider web-like dragnet traps tumor to limit its growth," Professor Rousseau said. He is convinced that using of Pept-in patented technology and aimed at the key disease for many diseases protein, they can design and synthesize the corresponding polymer molecules (amyloid protein structure of the characteristics of short-chain peptide sequence) to promote the pathogenic target protein to enhance cohesion and then fight many diseases. Because Pept-in patented technology makes use of the principle of amyloid formation to apply it to almost any target protein aggregation process. In the future, it can’t only be used to develop anti-cancer therapy, but also can be used against drug-resistant bacterial infection.

"In the next few years, our team will focus on using this technology to benefit more patients," Professor Schymkowitz said at the press conference. Flarebio offers recombinant proteins of good quality such as recombinant PIGR at great prices.

Scientists uncover how plants respond to drought at the molecular level

The sagging and drying of plant leaves suggests that we should water them, but how do plants respond to drought at the molecular level? Scientists at the Salk Institute have recently made a major breakthrough on this issue. This finding might help agricultural production adapt to adverse climates such as drought. The study was published in the Nov. 4 issue of Science. Studies have shown that in the face of unfavorable natural conditions, a small part of the plant proteins would act as a "command" to regulate the complex stress response. These experimental results were conducted using recombinant dog proteins and are expected to contribute to the development of new technologies for improving the use efficiency of plant water.

"At the molecular level, the response of plant to stress is a complex process involving hundreds of genes," said Joseph Ecker, author of the paper. "We have discovered a class of regulatory proteins that play a key role in plant responses to stresses such as drought. And if we can control a regulator protein, it's the equivalent of controlling all the genes it regulates."

Plant roots and leaves would secrete abscisic acid when water is scarce or salinity is high. "Only twenty or several regulatory proteins control the expression of hundreds or even thousands of genes," said Liang Song, the first author of the paper. "By identifying key regulatory proteins and studying their mechanisms of action, we can gain a deeper understanding and even regulate plant responses to stress."

In the experiments, the team at the Salk Institute tracked real-time changes in gene expression during plant secretion of abscisic acid and identified key regulatory proteins. These proteins control plant response to drought stress conditions such as stress response. By locating the binding sites of these regulatory proteins to DNA, they identified key proteins that can regulate gene expression networks, which can efficiently elicit a stressful response to environmental changes. This group focused on studying some of the known regulatory proteins that respond to abscisic acid.

During the experiment, they obtained 122 data sets containing 33,602 genes, of which 3061 genes had at least one time point of change in the expression intensity. Data analysis revealed a multi-level regulatory mechanism, in which regulatory proteins play a key role in gene expression regulation. Interestingly, the binding pattern of a protein at a particular time in DNA can explain much of the expression of a gene over a longer period of time. These kinetic properties together reveal that plant responses to environmental stimuli are a genome-wide synergistic response.

"Based on the understanding of the network structure, we found that a single key regulatory protein can control multiple components, which means that gene regulation is an accurate and interrelated process." Song said. "This is important for agriculture because it suggests that the control of one gene can activate or inhibit another set of genes, making it possible to design a human intervention program as a whole." This study suggests that this multi-level synergistic gene activity may be widespread in flower plants. Flarebio offers good-quality recombinant proteins such as recombinant CDH15 at good prices.

A new small molecule that can drive an extracellular-controlled hypoxic response

An international team has found through recombinant human proteins that a new small molecule called VH298 that can drive an extracellular-controlled hypoxic response.

The new study, led by Dundee University researcher Alessio Ciulli, is a new clinical approach that is critically important in the field of ischemic injury research due to brain and heart problems, as well as chronic kidney disease or chemotherapy-induced cardiovascular damage and anemia.

The use of small molecules in recent years is one of the research hot spots in new drug development, because it allows for the selective validation of new pharmacological targets and the rapid development of new compounds. However, the identification of these molecules is indeed more difficult.

According to the researchers, VH298 can inhibit the protein-protein interaction between the ubiquitin E3 ligase VHL and the HIF-1alpha transcription factor, a process similar to the selective control pathway that results in hypoxia in vivo. This work demonstrated for the first time that VHL protein as a drug intervention target. VH298 can stimulate erythropoietin (EPO) levels and resist hypoxia-induced injury.

Researcher Carles Galdeano, a member of the Computational Biology and Drug Design Research Group, graduated from the University of Barcelona School of Pharmacy with a PhD, and his previous research focused on neurodegenerative drug intervention.

Galdeano now focuses his research efforts on small molecule identification with biomedical roles in the proteasome ubiquitin system and is currently doing postdoctoral research. Flarebio offers recombinant proteins of good quality such as recombinant PIGR at great prices.

High-protein diet is good to your body and helpful to losing weight

Previous studies have shown that high-protein diet can help to lose weight - researchers now believe that they find the principle in it. Some studies have shown using recombinant mouse proteins that high-protein diet is good for you and also helps you lose weight. Researchers at the Imperial College in London have discovered the esoteric. Protein in the digestion process will produce an amino acid called phenylalanine. It will raise a hormone level, telling us that we've been full and we should reduce food intake.

The key to the problem is appetite. The release of phenylalanine from high-protein foods suppresses hunger. There are two sets of mechanisms. First of all, it will stimulate the body to create a hormone called GLP-1, which will inhibit your appetite, so you do not overeat. Second, it reduces the secretion of a hormone known as gastrin. The combination of both makes you feel fuller and hungrier.

The researchers did experiments in rats, injecting only one dose of phenylalanine and comparing them with mice that did not inject any material. They found that both hormonal levels were changed. When they gave obese mice a high-protein diet, these changes affect the body - mice eat less and began to lose weight.

In the final experiment, scientists used phenylalanine in human intestinal cells in culture dishes and observed the same process. Of course, the mouse and petri dish cells with the human body are huge, but this is still very convincing evidence. Mariana Norton, the first author of the paper, will present the study at this week's Congress of Endocrinology, which will then be peer reviewed and published.

Meat is a good source of protein, but not the only source. Other animal products (milk and eggs, etc.) and plants (spinach, tofu, amaranth, etc.) are excellent sources of protein. Flarebio provides superior recombinant proteins like recombinant Aoc3 at competitive prices.

Scientists discover new-type rearrangement mutations of B-ALL

Analysis of B-ALL carcinogenic mutations through recombinant horse proteins is of great significance for prognosis and treatment options. However, it is still not possible to identify the genetic basis of nearly 30% of B-ALL cases.

Researchers at institutions such as St Jude Children's Research Hospital recently conducted a transcriptome analysis of samples from more than a thousand B-ALL patients and found a new class of oncogenic rearrangements. These rearrangements all involve the MEF2D gene, the latter one may combine with at least six other genes (the BCL9 gene is the largest) after rearrangement, resulting in a fusion protein. The average age of patients with these mutations was 14, and the five-year disease-free survival rate was 71.6%. The researchers speculated that 5.3% of the currently unknown B-ALL cases in 30% of those carcinogenic mutations actually showed MEF2D gene rearrangement mutations. The findings are published in the recent issue of journal Nature Communications.

Panobinostat (Farydak) is an inhibitor of histone deacetylase (HDAC) and was approved by FDA in February 2015 for use in combination with bortezomib and dexamethasone to treat multiple myeloma. The researchers found that the HDAC expression levels of B-ALL cancer cells with MEF2D gene rearrangement mutations were significantly higher, and once it was administered panobinostat, its growth will be effectively curbed.

"In the past few decades, we have gained an in-depth understanding of the genetic changes that have led to ALL," said Dr. Stephen P. Hunger, Ph.D., author of The Children's Hospital of Philadelphia. "However, this study shows that we are still discovering new-type ALL subtypes. Gene mutations that occur in these ALL cancer cells will provide important information about therapeutic efficacy and accurate medical planning."

In addition to MEF2D gene, the researchers also found 20 patients with ZNF384 gene rearrangement mutations. ZNF384 protein is also a transcription factor. Among them, ZNF384 can recombine with other six genes to produce fusion protein. Analysis showed that B-ALL cancer cells carrying MEF2D and ZNF384 gene rearrangement mutations had a unique gene expression pattern. This suggests that the above fusion proteins are likely to be the key factors leading to cancer.

In the colony-forming experiments, the researchers also found that the MEF2D-BCL9 fusion protein could significantly enhance the proliferation of mouse lineage negative bone marrow cells by viral vectors, while the normal MEF2D or BCL9 protein did not.

"This suggests that the formation of MEF2D fusion proteins is a critical step in the transformation of leukocytes with limited longevity into infinitely proliferating leukemic cancer cells," said Dr. Charles G. Mullighan. Flarebio provides you with good-quality recombinant proteins such as recombinant TLR2 at great prices.

Scientists find the link between DNA and chronic joint pain

Scientists at King's College London have discovered a link between DNA modification and chronic generalized joint pain, one of the main symptoms of fibromyalgia, and the study is funded by the Arthritis Research Foundation. Fibromyalgia is a common chronic condition that causes muscle and bone fatigue and widespread pain. Although fibromyalgia is very popular, the etiology is little understood, and the treatments are limited. What's worse, fibromyalgia can't be detected using routine tests such as scanning or X-ray detection. The disease affects 4% of the world. The study, published in the journal PLOS ONE which also has other studies on recombinant dog proteins, will help scientists develop a diagnosis of fibromyalgia through blood tests.

"Fibromyalgia is affected by genetic factors, but there are a number of complex intermediate processes between genes and diseases," said Frances Williams, Ph.D., one of the authors of the article from the Department of Twin and Genetic Epidemiology. "Identifying measurable epigenetic associations is an important step. What's more, these results will provide information on future studies of fibromyalgia and other chronic pain syndromes, such as irritable bowel syndrome."

Stephen Simpson, director of the British Arthritis Institute, commented on the study, "Millions of people in the UK suffer from fibromyalgia, and this exciting study has helped us understand how individuals' epigenetic differences affect fiber Myalgia and chronic extensive musculoskeletal pain. For people with long-standing fibromyalgia, they have been struggling to diagnose their pain symptoms. This study will help to better understand, manage and treatment joint pain."

The researchers used twins to study whether DNA methylation affects the way genes start up when they produce a particular protein and to observe whether there are differences between musculoskeletal pain patients and non-patients. Scientists have determined that patients with chronic extensive pain and non-patients have different levels of DNA methylation in the three genes. Preliminary indications suggest that people may have different methylation patterns in their DNA and that this may affect the initiation of some genes and may lead to a variety of conditions. Flarebio offers superior recombinant proteins including recombinant Ptpra at good prices.

These antibiotics can also be cheaper and easier to treat tuberculosis!

Scientists have taken an important step in designing a new antibiotic to fight resistant bacterial infections, such as tuberculosis. In the study of natural chemical biology using recombinant mouse proteins, they described these new compounds to attack previous non-targeted enzymes, which are important for building and sustaining the cell wall of bacteria. The team said that these antibiotics can also be cheaper and easier to treat tuberculosis (TB).

The treatment of MDR-TB is costly. In addition, the treatment takes a long time and do harm to human body, and it has potentially life-threatening side effects. "One of the reasons for the new study is that more than half of the antibiotics given to patients today are of the β-lactam class," said Gyanu Lamichhane, associate professor of medicine at the Johns Hopkins University School of Medicine in Baltimore. These drugs paly their role by destroying DD-transpeptidase enzyme, while this enzyme is essential for the construction and maintenance of bacterial cell walls. Without enzymes, the bacteria die quickly.

However, about 10 years ago, the researchers discovered another enzyme called LD-transpeptidase - also important for the cell wall - is an antibiotic that allows bacteria such as TB to survive. In new research - in a complex imaging system, with the help of a protein called X-ray crystallography, the team investigated the detailed molecular structure of the LD-transpeptidase extracted from various bacteria.

With knowledge about the structure of the new enzyme, the researchers then tested the molecules that might work on it. They tested new compounds from beta-lactam antibiotic subclasses that specifically bind to new enzymes. By using live bacterial cultures, they show that compounds called carbapenems block wall-building enzymes. This also suggests that CDC, called the ESKAPE pathogen, works in a group of bacteria and is considered a particular threat because of its ability to resist drug resistance.

The team also tested two carbapenems in different groups of TB-infected mice. They found that even without the use of classical tuberculosis antibiotics, new compounds - especially ibuprofen - had a better therapeutic effect on tuberculosis in mice. "Our data show that carbapenem successfully treats tuberculosis infection by attacking enzymes," said Professor Lamichhane. The team is now planning clinical trials to test the safety and efficacy of some of these new compounds. Flarebio provides good-quality recombinant proteins like recombinant Itgb1 at competitive prices.

Scientists solve some puzzles of necrocytosis

Normally our tissues are healthy, but some of them will develop inflammation and disease. "What is it that causes inflammation? Is necroptosis the switch to inflammation? How does this process work?" said Manolis Pasparakis, professor of genetics at the University of Cologne, Germany. Professor Pasparakis' group of researchers published an article in the November 7 issue of Nature which also publishes other studies on recombinant horse proteins, partly answering these questions.

Professor Pasparakis' team constructed special skin cells: mice had RIPK1 lack in keratinocytes. The researchers had originally thought that the cells did not develop procedural necrosis due to RIPK1 deficiency, but the researchers got the opposite result: the cells keratinocytes in mice showed necrosis and died, triggering skin inflammation. By further analysis, the researchers found the answer. Because RIPK1 will inhibit another procedural necrosis factor: ZBP1 protein, genetic removal of ZBP1 can inhibit the RIPK1 deletion caused by necrocytosis and inflammation.

"We know that ZBP1 is a DNA-sensing protein that is involved in fighting the immune system of certain viruses but has yet to find its role in inflammation," said Chun Kim, co-author of the paper. So how does RIPK1 suppress ZBP1?

To answer this question, the researchers used the CRISPR gene editor to modify three amino acids in the RHIM domain, a key structure for the interaction of RIPK1 with two other proteins that regulate necrocytosis. Mice that express this mutated RIPK1 in all cells will not survive after birth. But only in the expression of keratinocytes will just lead to skin inflammation.

The researchers found that when RIPK1 PHIM domain shows mutations, ZBP1 will open necrocytosis, leading to perinatal mortality and adult skin inflammation. "This surprising result is that the three amino acids of RIPK1 can prevent ZBP1-induced necrosis, and it is the key to survival of mice and prevention of skin inflammation," said Juan Lin, one of the authors.

"We solved some of the puzzles, but there are bigger puzzles still unclear," Pasparakis said. "ZBP1 acts as a viral sensor, and now our study associates it with inflammation and death." In most cases, chronic inflammation in the human body is still a mystery. Why do some cases of inflammation in the human body happen? Our study found the important role of ZBP1. Now we wonder whether the virus or bacteria can activate ZBP1. The next step researchers will explore the further association of ZBP1 and inflammation in the human body. Flarebio provides you with good-quality recombinant proteins including recombinant ECEL1.

Keratins are endogenous ligands of DEC205

In November 7, 2016, the United States Academy of Sciences (PNAS) published a research result titled “Keratin mediates the recognition of apoptotic and necrotic cells through dendritic cell receptor DEC205/CD205” online and it was completed by He Yongning research group at the Chinese Academy of Sciences Shanghai Institute of life science biochemistry and cell biology Institute using recombinant human proteins, which discloses the molecular mechanism of immunoreceptor DEC205 / CD205 recognizing dead cells by binding to cytokeratin.

A large number of cells die in the human body every day. The identification of dead cells and clean-up is indispensable to maintain the body's homeostasis and avoid autoimmune diseases and is also an important function of the immune system. It is usually completed by dendritic cells, macrophages and other phagocytic cells. Phagocytic cells need to recognize dead cells through their surface receptor molecules. DEC205 (CD205) is one of the main markers and endocytotic receptors of dendritic cells and is widely used in immunotherapy. But its function is very limited understanding. Since the receptor was found in 1995, the cell ligand has not been found. In a previous study, the team found that the extracellular portion of DEC205 exhibited different conformations under acidic and basic conditions and that this conformational change was directly related to its function. DEC205 specifically recognizes apoptotic necrotic cells only under acidic conditions, thus revealing its physiological function as a dying cell receptor (PNAS, 2015). However, how DEC205 recognizes dead cells is still unclear.

In this work, on the basis of previous results, Cao Longxing and other researchers looked for human DEC205 on the cell ligands through a series of biochemical and biophysical experiments. As a result, it was found that keratins are endogenous ligands of DEC205. Further experiments have shown that the human DEC205 molecule can specifically recognize the C-terminal domain of keratin by its N-terminal domain under acidic conditions. Keratin is an important component of the cytoskeleton and usually can form fibrous intermediate filaments involved in the maintenance of cell morphology and mechanical properties, but other physiological role of keratin is not very clear. This work shows that keratin not only plays an important role in maintaining the cell and tissue structure, but also as a marker of cell death and is recognized by the immune system and mediates an acid-base-dependent death cell recognition pathway. In addition, keratin and tumor also exist between the close contact and is used for clinical diagnosis of a variety of tumors. Therefore, the finding of DEC205 as a keratin receptor provides a new way of thinking for diagnosis and treatment of cancer and related diseases. Flarebio offers good-quality recombinant proteins such as recombinant ITGB5 at competitive prices.

Scientists discover an antimicrobial peptide to destroy drug-resistant bacteria

In order to deal with the arsenal of bacteria, scientists have taken various different approaches. They no longer develop and improve traditional antibiotics but look to some of the natural antimicrobial substances through recombinant dog proteins. Some of them are fragments of proteins, known as peptide. Recently, researchers from the Massachusetts Institute of Technology, University of Brasilia and the University of British Columbia in Canada designed an antimicrobial peptide that can eliminate many bacteria, including drug-resistant bacteria. This result was published in the Nature Publishing Group Scientific Reports.

Many organisms naturally produce antimicrobial peptides, which are part of the body's own immune system, not only to destroy invading bacteria, but also kill other microorganisms, including fungi and viruses. They have the advantage of acting on bacteria through a number of different mechanisms. First, they can drill holes in the cell membrane that invades the bacteria and can destroy multiple targets, including DNA, RNA, and proteins when inside the bacteria. Second, they can activate the body's own immune system and call the white blood cells to completely eradicate the invasion of microorganisms. This is also the biggest difference between these peptides and traditional antibiotics. In addition, they can also inhibit the immune system due to excessive systemic sepsis.

Naturally-produced antimicrobial peptides are usually composed of 20 amino acids, which include a positively-charged region to help punch in the cell membrane and a hydrophobic region so that it can smoothly go through the cell membrane into the bacteria inside. With the development of modern computing technology, scientists can replace or add new amino acids to transform the natural antibacterial peptides and even design and manufacture of new antibacterial peptides so that they become more lethal.

In this study, the scientists improved based on antibacterial peptide clavanin-A found in the body of a marine organism sea squirt, including the addition of five hydrophobic amino acids to make the entire polypeptide more easily to go into the bacteria. They called the new antibacterial peptides clavanin-MO. In mice, clavanin-MO was found to abolish resistant E. coli and Staphylococcus aureus strains. It also destroys biofilms formed by bacteria on the surface of objects, such as biofilm formed by Pseudomonas aeruginosa found in the lungs of patients with cystic fibrosis.

"Our goal is to find solutions to antibiotic resistance," said Cesar de la Fuente, Ph.D., one of the authors of the paper. Drug-resistant bacteria are expected to exceed cancer and become the number one killer of human health. Antibacterial polypeptide provides an effective alternative: a molecule that can kill resistant bacteria and boost immunity and prevent excessive immune responses."

The researchers plan to further improve the design of antibacterial peptides and eventually put into clinical use. They believe that if combined with traditional antibiotics, it can be more effective in the eradication of bacteria and prevent new drug resistance. Flarebio offers good-quality recombinant proteins like recombinant CDH11.

The key genetic switch in the liver has the function of regulating glucose metabolism

Researchers have recently discovered that the key genetic switch in the liver has the function of regulating glucose metabolism and insulin secretion in other organs through recombinant mouse proteins.

Diabetes is a chronic disease. Now, the incidence of diabetes is becoming more and more serious. In Germany, more than 6 million people suffer from this disease. Diabetes is characterized by impaired glucose metabolism (with the exception of type 1 diabetes) as well as by the body's response to insulin. Scientists are currently looking for possible causes of the disease and modulators that could be used to intervene therapeutically.

Currently, a team led by Professor Stephen Herzig has discovered a new mechanism responsible for mediating glucose metabolism. Transforming growth factor-β1-stimulated clone 22D4 (abbreviated as TSC22D4) acts as a molecular switch in the liver and regulates the effects on the systemic metabolic genes.

“As early as 2013, researchers have shown that increasing the expression of TSC22D4 in the liver of cancer mice can lead to severe weight loss,” study leader Herzig said. In this study, researchers have studied the role of this gene modulator in diabetes.

In the current study, the researchers found that TSC22D4 inactivation can improve insulin resistance and glucose metabolism. Further study showed that TSC22D4 can inhibit the formation of apolipoprotein 13. This protein can be released as a messenger material from the liver and regulate other organs of glucose metabolism.

In order to examine the new mechanism and clinical relevance of this finding, the researchers examined 66 patients with type 2 diabetes or healthy liver. The results showed that in the liver of diabetic patients, TSC22D4 gene expression was more than normal, and the synthesis of corresponding reduction in apolipoprotein 13 reduced. "The results of the study help to find new ways to treat diabetes," the researchers said. Flarebio offers recombinant proteins such as recombinant CDH11 at competitive prices.

A new immunotherapy technology that can completely reverse allergic reaction in mice

In the best of cases, food allergy can only be frustrating; while in the worst case, food allergy can be life-threatening. Recently, however, scientists have developed a new immunotherapy technology that can completely reverse the allergic reaction in mice and the research used a lot of recombinant proteins including recombinant rat proteins. They believe that this technology can also be used for the treatment of human allergies. This treatment technique works by triggering the body to produce new dendritic cells that can tell other immune systems to stop the excessive immune response. This ensures that the quickest and most severe types of allergic reactions will not occur.

"If we can use this new therapy to reliably treat food allergies or related diseases such as asthma or autoimmune diseases (such as multiple sclerosis)," says John Gordon, a scientist at the University of Saskatchewan in Canada, then it will change the lives of many affected people."

Dendritic cells are naturally generated in tissues exposed to the environment, such as the lining of the skin or nasal cavity, lungs, stomach and intestine. Gordon and his team extracted the cells from mice and exposed them to a specific mixture of proteins, a naturally occurring vitamin A-related acid in the human digestive system, and an allergen (peanut or egg white).

When these modified dendritic cells were re-implanted in mice, the allergic reaction in mice almost disappeared, and the sensitive immune cells activated by allergic substances have been like in healthy and non-allergic the human body. Although the technology has currently been tested only in mice, the researchers hoped to be able to carry out human trials next year. "We have a lot of people with allergies who are willing to give their cells to us for testing," Gordon said.

The effective treatment of allergies can change the lives of millions of people. In the United States alone, there are an estimated 15 million food allergy sufferers, and one in 13 children suffers from some kind of allergy. The team believes the study could also be used for other diseases associated with the immune system such as multiple sclerosis (MS). Gordon explained that only a few changes can be applied to the treatment of autoimmune diseases.

The study was published in the Journal of Allergy and Clinical Immunology. Flarebio provides you with superior recombinant proteins including recombinant CDH2.

A study shows new method of inhibiting cancer genes

Researchers at the University of Illinois at Chicago have discovered a new way to stop the mutations in nearly 30% of cancer patients through recombinant human proteins. Gene mutations in the RAS family of proteins are present in nearly 90% of pancreatic cancer patients and are also prevalent in patients with colon, lung and melanoma (the most dangerous skin cancer). The histone consists of three members: K-RAS, H-RAS and N-RAS.

The prevalence of RAS mutations in human cancers and the dependence of RAS on tumor survival make RAS a major target for cancer research and drug discovery. Scientists and drug developers have long sought RAS oncogene to find a new way to treat cancer, but they have yet to find a drug that can safely inhibit the activity of oncogenes.

A team led by John O'Bryan, an associate professor of pharmacology at the University of Chicago School of Medicine, took a different approach to RAS and found that a synthetic binding protein called NS1 monobody which they synthesized in the laboratory can block the activity of RAS protein.

"We did not find a drug or a specific inhibitor," says O'Bryan, a member of the University of Illinois Cancer Center, who met at the Jesse Brown VA Medical Center in Chicago, "We use monoclonal antibody technology, a protein engineering technique, to identify regions of RAS that are critical to its function. Unlike traditional antibodies, which do not rely on their environment and can easily be used as inhibitors of gene coding Agent."

"The beauty of this technique is that when a mAb binds to a protein, it's usually acting as an inhibitor of the protein," he said. The monoclonal antibody was developed by Shohei Koide, a professor of biochemistry and molecular pharmacology at New York University and co-author of the study. They are used for different proteins, including enzymes and receptors.

The researchers found that NS1 monobody binds to a region of the RAS protein molecule that is not previously thought to be important for carcinogenic activity. NS1 strongly inhibits carcinogenic K-RAS and H-RAS by blocking the ability of the protein to interact with another identical protein to form a molecule. NS1 does not affect gene N-RAS.

O'Bryan said these findings of biology and chemistry published in The Wall Street Journal provides important insight into the long-standing problem of RAS protein function in cells. These insights can help to guide the development of new methods of treating cancer by interfering with cancer cell mutations in RAS function.

"Developing an effective RAS inhibitor represents a holy grail in cancer biology," O'Bryan said. "We now have a powerful tool that we can use to further investigate RAS functions. Although these findings will require much research and effort to be used outside of the laboratory, this study provides new insights on how RAS slows down tumor growth." Flarebio offers recombinant proteins of good quality like recombinant Phex.

How do plant seeds fool beetles?

We have seen many animals survive by being camouflaged to avoid being eaten by their predators. But have you seen any plants protect themselves by mimicry? A team consisted of researchers from both University of Cape Town and the University of KwaZulu-Natal in South Africa, has found an example of that - a seed from a plant uses mimicry to fool a beetle. They published their paper in the journal Nature Plants, which also have other studies on recombinant rat proteins. In their paper they describe the relationship between the seeds and the beetles and the deceptive dispersal they witnessed through observation.

In fact, many examples of animals or plant mimicry have been noted and reported in studies published before, but until now, no examples of a plant using mimicry to disperse seeds have been documented. The research which seeds of a grassy plant known as Ceratocaryum argenteum were somehow dispersed used to draw public attention, but no one had figured out how it was occurring. The researchers write that they believed it was because mice carried them about. To make sure about the guess, they dropped 195 of the seeds near monitoring stations in De Hoop Nature Reserve and recorded what happened with video cameras.

Over a single day, dung beetles moving through the area had grabbed nearly half of the seeds and rolled them to nearby locations where they buried them later. As you know, dung beetles normally grab animal droppings and bury them for eating or use them for a place to lay eggs.

Subsequently, the researchers dug up all the seeds which were buried by the beetles and found no traces of beetles around, let alone any eggs laid by dung beetles. The results suggested that those beetles discovered the ruse as they attempted to eat them or lay eggs. Therefore, the team guessed that the dung beetles had been fooled into carrying the seeds to a distant places and planting them and got no reward for their efforts.

They inspected the seeds and found that they looked like bontebok dung a lot. What's more, the chemical composition of the seeds closely resembled dung as well. It must be the smell of the seeds that fools the beetles. Flarebio provides you with superior recombinant proteins including recombinant Cd44 at competitive prices.