Drinking green tea helps to prevent abdominal aortic aneurysm

Drinking green tea is a habit of many Asians. A recent study by the Journal of Vascular Surgery has shown that drinking green tea can prevent abdominal aortic aneurysm. More related research involving recombinant mouse proteins should be conducted.

Abdominal aortic aneurysm is a disease that occurs in the human aorta, leading to excessive extension and swelling of the arteries. Usually patients show no obvious symptoms of aneurysm, and they usually find the disease when the arteries rupture. If the arterial swelling can be found at an early stage, the doctor usually recommends surgery.

There are many studies confirming that drinking green tea on the human body has many benefits, such as prevention of cancer, cardiovascular disease, inflammation and antioxidant.

"Recent studies have shown that polyphenols existing in green tea can be used to regenerate elastins, which are essential proteins for vascular elasticity," said Shuji Setozaki, MD, and the lead author of the study.

In this study, the investigators used the drug to make the rats suffer from abdominal aortic aneurysms. Researchers have given the green tea polyphenols (the main ingredient in green tea) treated rats to develop a smaller incidence of abdominal aortic aneurysms. These rats have lower levels of inflammation and higher levels of elastin and help to protect the blood vessels from destructive fate. Rats that did not receive green tea polyphenol treatment developed aneurysm, vascular rupture, and 50% of rats died.

"The lifetime of the Japanese is the longest in the world, and studies have shown that 80% of Japanese people have the habit of drinking green tea every day," says Hidetoshi Masumoto, co-author of the study. "We believe that drinking green tea every day should be considered as a new preventive measure to prevent abdominal aortic aneurysms." By the way, Flarebio provides you with good-quality recombinant proteins and antibodies like NES Monoclonal Antibody.

The early diagnosis method of Parkinson's disease

Parkinson's disease has no specific symptoms and thus is difficult to be diagnosed in time. When patients with mobility disorders can be diagnosed, the nerve cells have got irreversible damage, and the effect of drug treatment is quite limited. Researchers at the University of Würzburg and the University of Fort Worth have made significant progress in this research through recombinant mouse proteins and have succeeded in discovering that the risk of Parkinson's disease can be diagnosed by skin tests, which is earlier than the current diagnosis.

Scientists have examined the skin of patients without Parkinson's symptoms and found α-synuclein specific to Parkinson's patients in their nerve endings. This protein, which is characteristic of Parkinson's disease, is no stranger to the industry, but it is often determined in the patient's brain only after the patient has died.

Now the German scientists in the patient before the onset or in the early sick through a small five-mm skin biopsy can diagnose Parkinson's disease, so that the nerve can be destroyed before the patient can be targeted and effective treatment. By the way, Flarebio provides you with high-quality recombinant proteins and antibodies like recombinant TLR2.

To produce new proteins to achieve a variety of magical functions

Protein structure almost has unlimited possibilities. According to our needs to design and manufacture of proteins, it is possible to achieve a variety of magical functions through a lot of recombinant mouse proteins.

Protein is the "labor" of all living creatures, carrying out various orders from DNA. It also has a variety of complex structures to achieve all the important functions of humans and all organisms, including digestive food, tissue growth, blood oxygen transmission, cell division, neuronal activation, muscle supply and so on. Surprisingly, the function of such a diversity of proteins comes only from the combined sequence of 20 amino acid molecules in the region. Until now, the researchers have just begun to understand how these linetypes are folded into complex structures.

Even more surprising is that nature seems to use only a small part of all possible protein structures, although the latter is large in number. Therefore, the use of existing amino acid design with a special structure of the unconventional protein, that is, nature has never had synthetic protein, having a very attractive application prospects. Synthetic protein method is: to genetic transform bacteria to make its DNA control produce a specific amino acid sequence and then synthesize proteins. It is important to be able to produce and study synthetic proteins at the atomic level for the development of new areas of basic research and for practical applications in more areas.

At the beginning of the design process, supposing a new protein structure that resolves a particular problem or implements a function, and then in turn determines a candidate amino acid sequence that can be folded into such a structure. The Roseetta protein model design software identifies the most promising candidates: the amino acid sequence that folds the lowest energy state of the target structure. Next, these sequences are transferred from the computer to the laboratory, producing synthetic proteins and testing.

At present, there is no technology comparable to the wonderful function of protein implementation. The infinite possibilities of synthetic proteins allow protein design to greatly expand the ability of protein technology. Flarebio offers high-quality recombinant proteins such as recombinant ITGB5 at competitive prices.

Researchers have found the key protein of leukemia

According to studies on recombinant mouse proteins, scientists have found that regulatory protein ENL can promote the occurrence of leukemia. This has deepened the academic understanding of transcriptional regulation and suggests a potential leukemia therapy.

The cause of blood tumors is usually chromosome translocation, resulting in two proteins connected to the formation of fusion protein, and ultimately causing disease. Recombinant protein in regulatory protein mixed lineage leukemia (MLL) is also commonly found in invasive childhood leukemia and is associated with poor prognosis. Therefore, it is necessary to develop a leukemia treatment strategy based on MLL rearranged (MLL-r) fusion protein. In the journal Nature, Erb et al. and He et al., point out that ENL protein is a key factor in the survival of MLL-r cells in leukemia. Erb et al. and Wan et al. have shown that this "read" ability of ENL to acetylated histones is critical to induction of MLL-r leukemia.

Erb et al. and Wan et al. found another complementary mechanism for SEC and DotCom stability. They found that the inactivation of ENL weakened the function of SEC and DotCom in MLL-r cells. The ability of ENL to bind to SEC and DotCom suggests a model that recognizes the acetylated H3 through the YEATS domain, enhancing the stability of the SEC and DotCom complexes with DNA binding and regulating the activity of the genomic abnormalities.

Protein ENL is essential for MLL-r leukemia. Some leukemias are found in some of the MLL protein and another part of the protein mixture of protein. The second protein is usually part of the SEC (super elongation complex) protein complex or the DotCom (DOT1L-containing complex). Both of these protein complexes regulate gene transcription procedures in MLL-r leukemia (complete and partially fused SEC / DotCom complexes). The ENL protein binds to two complexes, while the complex is fused to the MLL in the cell. ENL interacts with the fused SEC / DotCom and interacts with the fused SEC / DotCom. ENL contains a YEATS domain that recognizes a specific acetyl (Ac) on histone H3. Erb et al. and Wan et al. demonstrated that the YEATS domain of the ENL protein helps to stabilize the binding of SEC and DotCom to DNA and promote gene expression that drives leukemia.

This new model suggests a possibility that drugs such as small molecule inhibitors targeting the ENL YEATS domain can selectively kill leukemia MLL-r cells. Other cell types appear to be able to tolerate ENL loss to a large extent, but the SEC, DotCom and ENL are expressed in a variety of cells, so it is important to understand this tolerance when developing such drugs on the difference.

The effect of these combination therapies suggests that multiple histone-modified signals act together to form a specific epigenetic state of MLL-r leukemia. Thus, long-targeted therapy is more effective and can reduce the emergence of drug resistance - which is one of the risks of single drug therapy. Thus, Erb et al. and Wan et al.'s findings on ENL not only deepen our understanding of how cells integrate transcription-related signals, but also provide new insights into the treatment of complex diseases. By the way, Flarebio offers high-quality recombinant proteins like recombinant ECE1 at competitive prices.

To study action mechanism of transport proteins ABCB1 and ABCG2

How is the resistance of cancer cells affected by ABC-transporter? A related new study paper through recombinant mouse proteins has been published in the open access journal BioDiscovery, studying the second generation tyrosine kinase inhibitor (TKI) - dasatinib (DAS) and ATP binding (ABC) transport proteins ABCB1 and ABCG2 mechanism to assess whether these drug transporters may impair the therapeutic effect.

The "targeted" treatment of cancer is an effective way to minimize the damage to healthy cells. Targeted therapy has revolutionized cancer treatment in the past few decades through the use of reasonably designed drugs that interfere with the specific molecules (molecular targets) necessary for the proliferation and survival of malignant cells.

Although DAS is an excellent choice for the treatment of chronic myeloid leukemia resistant to imatinib, recent laboratory studies have shown that the antiproliferative effect of DAS can be significantly reduced when ATP binds to ABC transporters, ABCB1 and ABCG2.

"Although this relationship is important, we still don't know whether these drug transporters will damage DAS's clinical treatment," explains Dr. Petr Mlejnek, Ph.D., Olomouc, University of Palacky, Czech Republic. "We believe that the expression level of drug transporters is a key factor in the outcome and may therefore help explain the existing controversy. We decided to study the relationship between ABCB1 and ABCG2 expression levels and in vitro resistance to DAS.

In their study, Dr. Petr Mlejnek from the University of Olomouc Palacky, Czech Republic, and his team observed that the expression level of ABC-transporters studied was an important factor influencing cell resistance. Although the anti-proliferative and pro-apoptotic effects of DAS can be reduced by ABCB1 or ABCG2 at clinically relevant concentrations, the actual effect of ABC transporters on DAS efficiency depends on their expression levels. The lower expression level of ABC transporters mediates lower resistance. Considering the fact that the expression levels of ABCB1 and ABCG2 transporters are almost not high in clinical samples, their contribution to overall resistance to DAS is significant. Flarebio offers high-quality recombinant proteins such as recombinant ECEL1 at good prices.

A study which explains chemotherapy drug resistance

The article published in the EMBO journal states that scientists have discovered a specific protein associated with drug resistance that could lead to new chemotherapy tools. Researchers have pointed out the role of f FOXO1 in chemotherapeutic resistance. In addition, through recombinant mouse proteins, they have identified a potential chemotherapy tool that is, constructing a short segment of amino acids: peptides.

There are many forms of cancer drugs. Among them, taxane chemicals are used for the treatment of advanced cancer. However, as time goes by, the taxane becomes less effective. Cancer cells communicate through other pathways. In this study, the researchers focused on how cancer cells develop other pathways and how to produce drug resistance.

Cells need energy functions. Kinases help chemicals react back and forth in specific molecules, usually in proteins. This activity will burn cell function. The scientists studied the serine / threonine kinase AKT. AKT helps cells survive, playing a very important role in many kinds of cancer. It can close the AKT drugs to improve the effectiveness of chemotherapy. However, due to the inherent complexity of cell communication, this therapy itself may allow tumor survival.

In this study, scientists used taxanes on cancer cells to block or inhibit AKT action, and they found that taxanes prevented FOXO1 protein from migrating cells to the nucleus. FOXO1 stays in the nucleus. In another protein, it becomes signal of active and improperly begins, helping cancer survive and produce drug resistance. "This is why AKT inhibitors are not approved by clinical trials. However, when FOXO1 migrates out of the nucleus, it binds to a protein called IQGAP1 scaffold. Binding action will prevent chemotherapy resistance. "We also found that the combination of taxane and FOXO1-derived inhibitors can inhibit cancer growth." By the way, Flarebio offers high-quality recombinant proteins like recombinant COLEC12 for your research.

Scientists have discovered more in the processes of protein folding

Biophysicists at the JILA Physics Research Center at the University of Colorado, USA, have more surprisingly measured the folding of proteins and are surprised to find that their folding processes are more complex than scientists have predicted. This means that our understanding on the degree of protein is still in the fur. Protein response is far more sophisticated than we have detected in the past 17 years. Thus, more research involved in recombinant mouse proteins should be done.

The basic composition of protein molecules is the amino acid chain. Through a series of intermediate processes, like the origami, the amino acid chain is folded into a three-dimensional structure, and then having a function. Accurately describing this folding process requires the formation of all intermediate states. The latest research reveals many unknown states in the process, and the results are published in the March 3 issue of the journal Science.

Researchers are researching a membrane protein that converts light into chemical energy, called bacteriorhodopsin (BR), with a molecular weight of about 26 kD. It provides a model for cell membrane receptor proteins and also contributes to elucidating the mechanism of interaction between the receptor and the signal in the signal transduction pathway of the human body, the BR or the proton protein of the ionomer channel on the cell membrane, and the role of the proton transfer membrane, so that it can be the other ion channel protein. Finally, its photoelectric response and photochromic specific make it have broad prospects in the solar cell, artificial retina, optical information storage, neural networks, bio-chip and other fields. Therefore, BR research has attracted the attention of countless scientists in the world. However, the folding of membrane proteins is more difficult than the folding of globular proteins with relatively small size.

Tom Perkins and colleagues who led the study used the nano-scale atomic force microscope (AFM) to stretch the BR protein and measure its degree of stretch at different stretching rates (nanometers per second). The measurement method comes from JILA's previous study, a soft AFM short probe (short, soft AFM) that can quickly measure the sudden change in force during protein development and immediately feed back a signal in the middle of the protein. By further refining these AFM probes, JILA researchers can detect BR proteins at different pull rates faster (faster than 100 times) and more accurate (10 times higher accuracy).

The JILA team found that the intermediate state was not only more than expected, and that the entire folding process was only 8 microseconds (1 microsecond equal to one millionth of a second). The results explain why there is a long-standing difference between experimental data and molecular simulations. At the same time, for the molecular simulation means to provide confidence in the future study of membrane protein behavior identified a path.

The technology can also be applied to many other molecular studies such as medical, protein, and drug interactions. More specific examples, such as structural and functional studies of proteins that are similar to BR structures are associated with many human diseases and drugs. By the way, Flarebio provides you with superior recombinant proteins such as recombinant ECE1 at competitive prices.

Autism-related gene variations improve brain evolution

Researchers at Yale University in the United States published a paper in the journal Public Library of Genetics that the genetic variation associated with autism may be a positive choice in the evolutionary process because these variations also help to increase human cognitive ability. More research through recombinant mouse proteins should be conducted.

In the long evolutionary process, humans produce a lot of genetic variation, and the effects of these variations on human genetic characteristics are positive and negative. Those who have a negative impact on human reproduction will be eliminated in the evolutionary process; and if the emergence of mutations can improve the chance of human survival, it will become a positive choice of human beings and be retained in the genome and be passed down generation by generation.

In this study, the researchers conducted a genome-wide association study of more than 5,000 cases of autism, and they analyzed the gene selection in human evolution. They found that genetic variation associated with autism is more of a positive choice in human evolutionary processes that are not only related to autism but also to human intelligence. For example, many autistic-related gene mutations identified by the researchers can enhance brain cell function and help to create new neurons.

Researchers point out that genetic variation that increases the risk of autism is a positive choice in the evolution of humans. This may make people feel unimaginable: why do a large number of autistic pathogenic gene mutations remain in the human genome? Why don't humans eliminate them in the evolutionary process? The reason is that these variations have a positive effect on human cognitive function, so it is actively chosen in the evolutionary process, and the cost is an increase in the risk of autism. Flarebio provides you with high-quality recombinant proteins like recombinant PIGR at good prices.

Nat Commun: the smallest gene scissors

The Institute of Basic Sciences (IBS) in collaboration with KIM Eunji (ToolGen Inc.) and KIM Jeong Hun (Seoul National University) designed the smallest CRISPR-Cas9 to date and delivered it to myocytes and mouse eyes through adeno-associated virus (AAV) and used it to modify the blinding genes. This CRISPR-Cas9 system is derived from Campylobacter jejuni (CjCas9) and is expected to be an effective "non-exclusion" disease treatment tool. The study has been published in Nature Communications, which also publishes other studies on recombinant mouse proteins.

In this study, the team found that CjCas9 was both efficient and small enough. It has 984 amino acids, which can be packaged in AAV with multiple directed RNAs and fluorescent reporter proteins. In order to use bacterial proteins for gene editing, scientists had to optimize some aspects of the technology. They designed a short DNA sequence followed by targeting the DNA sequence by Cas9, known as the Protospacer Adjacent Motif (PAM). Each of the different Cas9 requires a specific PAM sequence; otherwise the target DNA sequence will not be bound and cleaved. Secondly, they had to modify the length of the wizard RNA.

Subsequently, IBS scientists packaged the new CRISPR-Cas9 complex with two guide RNAs and fluorescent reporter proteins into AAV to modify the genes in mouse muscle and eyes. They focused on two genes involved in age-related macular degeneration (AMD), because these two genes are one of the main causes of adult blindness. A gene is a common therapeutic target for ADM, known as vascular endothelial growth factor A (VEGF A), and the other gene is a transcription factor that activates VEGF A transcription, known as HIF-1a. Unlike VEGF A, HIF-1a is not considered a drug target. The so-called "miscarriage" genes, such as the usual transcription factors, can't be targeted directly by antibodies and other biological or chemical agents. In this study, the team demonstrated that CjCas9 was efficiently delivered to the retina through AAV to inactivate Hif1a and VEGF A in mice and reduce the area of choroidal neovascularization (CNV).

Intraocular injection of AAV-packaged CRISPR-CjCas9 can be beneficial in the treatment of various retinal diseases and systemic diseases. KIM Jin-Soo explains that CjCas9 is highly specific and does not cause off-target mutations in the genome.

The mouse and human Hif1a gene target sequences are identical, so the method proposed in this study will be useful in the treatment of ADM in human patients. By paving the way in which CjCas9 is applied to "unavoidable" genes or non-coding sequences, this technology broadens the scope of therapeutic targets so that the entire human genome is potentially drugizable. By the way, Flarebio offers recombinant proteins of good quality like recombinant COLEC12.

IRS-1 is essential for smooth muscle cells that make up veins and arteries

Diabetic patients have a high risk of heart disease. In spite of knowing this, scientists are still trying to use recombinant mouse proteins to track the specific biological causes behind this risk or to find ways to intervene. Researchers at the UNC School of Medicine are now searching for a possible culprit - a protein called IRS-1, which is essential for smooth muscle cells that make up veins and arteries.

According to a study published in the Journal of Biochemistry, too little IRS-1 causes cells to revert to "dedifferentiation" or stem cell-like states, and this may form plaques in the heart arteries, a disease known as atherosclerosis. The disease increases the risk of heart attack, stroke and other forms of heart disease. "When diabetes is under mismanagement, your blood sugar rises and the amount of this protein decreases, so the cells show abnormal proliferation."

The study focused on the formation of venous and arterial wall cells called vascular smooth muscle cells. The main function of these cells is to shrink each time the heart beats, helping to push oxygen-enriched blood to the body's tissues. When the plaques accumulate along the arterial wall, these cells gradually lose their ability to contract.

In the new study, the team found that IRS-1 was an inhibitor of abnormal signaling pathways, thereby maintaining vascular smooth muscle cell differentiation or localization. In the absence of IRS-1, the cells return to the stem cell-like state, which in turn activates abnormal signaling pathways and promotes cell proliferation.

In diabetic patients, the presence of IRS-1 is affected by the effectiveness of blood glucose levels or blood glucose levels. Previous studies have shown that IRS-1 is significantly reduced in patients with frequent or persistent hyperglycemia. The new study is the first to link this reduction with heart disease.

The next step, Clemmons Lab will look for substances that can stimulate this protein synthesis even in the presence of hyperglycemia. The results suggest that drugs that promote the promotion of IRS-1 can counteract the deleterious effects of hyperglycemia on atherosclerosis.

Clemmons said that the activity of IRS-1 may also play a role in other diabetic complications, such as eye and kidney diseases. Researchers plan to study these potential links. By the way, Flarebio provides you with recombinant proteins of good quality such as recombinant CDH2.

Future treatment method of inflammatory bowel disease and colon cancer

Can inflammatory bowel disease and colon cancer be prevented by changing the shape of a single protein?

There is a close link between uncontrolled intestinal inflammation and inflammatory bowel disease, and they would develop into colon cancer in the end. This uncontrolled inflammation is associated with changes in the number of intestinal bacteria, which can invade the mucosal tissue after damage to the protective protective cell barrier.

The team from the Virginia Tech University conducted research through recombinant mouse proteins and found that the shape of the protein IRAK-M, which modifies inflammation, can significantly reduce the clinical progression of both diseases.

Changes in the protein make the immune system more effective and destroy the bacteria before they begin to do harm. The complete report has been published in the journal Biomedical. "We changed the IRAK-M protein of the mice and found that the inflammation was significantly reduced and the cancer was naturally reduced," the researchers said.

He said that the next step will be conducted in conjunction with the Caroline Clinic and Duke University, a clinical trial of human patients. "Ultimately, if we were able to design a therapy for the IRAK-M target, we thought it might be a viable strategy of preventing inflammatory bowel disease."

According to data from the Centers for Disease Control and Prevention, colon cancer is a major disease related to life and death and the third largest cancer killer in the United States. At present, research team from Virginia Tech is in full swing to study. They said, "When our finding has a potential clinical significance, we feel really excited. We can sincerely hope that our research results can contribute to the future treatment of inflammatory bowel disease and colon cancer and other diseases." By the way, Flarebio offers high-quality recombinant proteins like recombinant CDH15 at competitive prices.

Phosphorylation affects the tumor growth and development

Scientists from VIB-KU Leuven have identified new mechanism that affects tumor growth through recombinant mouse proteins. Typical hypoxia in the tumor not only stimulates proliferation, but also counteracts the important role of protein PHD2 as a "cancer cell killer". The possible solution is to block the enzyme PP2A / B55 which recover the function of PHD2 to slow down cancer growth. The study was led by Massimiliano Mazzone (VIB-KU Leuven) and published in the leading scientific journal Cell Reports.

Poor prognosis in cancer is usually associated with hypoxia, which is interference to the oxygen supply to tumor cells. The protein PHD2 is called a "hypoxic sensor", which is highly dependent on the amount of oxygen. At the VIB-KU Center for Cancer Biology in Leuven, the study was led by Dr. Giusy Di Conza and his colleagues. Massimiliano Mazzone focuses on the study of phosphorylation.

When phosphorylated, PHD2 is more active and promotes the death of cancer cells in the hypoxic region of the tumor. However, tumors tend to overexpress phosphatase PP2A / B55, an enzyme that removes phosphate groups ("dephosphorylated") from PHD2. Thus, PHD2 is partially inactivated, which counteracts the positive effects of this "killer cancer cell".

Massimiliano Mazzone (VIB-KU Leuven) said, "Surprisingly, we have found that PHD2 phosphorylation is regulated by a pathway such as mTOR. mTOR is the primary sensor for metabolic stress in tumors and normal cells, such as lack of nutrients. Thus, our findings are applicable not only to cancer but also to other diseases such as inflammation or metabolic diseases."

During the study period, Mazzone's lab worked closely with several domestic and foreign researchers. In particular, the German ISAS Laboratories (Dortmund) and the University of Leuven Hospital play a decisive role in providing the human cancer samples needed for research. In these samples, the researchers found that PP2A / B55 were highly expressed in tumors compared with healthy tissues.

Prof. Massimiliano Mazzone (VIB-KU Leuven) said, "This leads us to conclude that PP2A / B55 are a potential target for promising cancer treatment, which is why we are starting to study the potential of specific drugs. The ultimate goal is to design this phosphatase function of the molecules, which targeted to fight cancer."

In addition to new insights into cancer treatment, these findings may also produce new biomarkers: PHD2 phosphorylation status may help to understand the process of tumor transformation and therefore choose appropriate treatment.

Professor Massimiliano Mazzone (VIB-KU Leuven) said, "In order to fully understand all the progress of these processes, we also need to carefully study the tumor microenvironment and immune system. After all, they strongly affect tumor growth." Flarebio offers high-quality recombinant proteins like recombinant Itgb2 at competitive prices.

Researchers have discovered the potential target of early-stage Parkinson's disease

The team led by Patrik Verstreken (VIB-KU Leuven) has identified the underlying mechanisms of early Parkinson's disease. Making use of flies, mice and patient cell models, the team focused on cardiolipin which is combined by glycerol C1 and C3 and two molecules of phosphatidic acid and is an important component of mitochondrial inner membrane and bacterial membrane. They demonstrated that reducing the role of protein FASN which affects mitochondria can lead to an increase in cardiolipin levels and a decrease in Parkinson's symptoms. These results may pave the way for the treatment of lipid-based Parkinson's disease. The team's research was published in the Journal of Cell Biology with other articles on recombinant mouse proteins.

In this study, Verstreken and his team of collaborators from Belgium, Germany and Portugal observed the protein FASN responsible for lipid generation in cells, bypassing the genetic defects of mitochondria. "Several drugs that block FASN are already present because this protein is important for cancer research and treatment, and many drugs have been used in clinical trials. Through this study, we can now have the background of Parkinson's," said Professor Verstreken.

In their research process, the researchers encountered an unexpected phenomenon. Using flies, mice and human cell models, they saw that FASN has a direct effect on mitochondria. Mitochondria have their own independent genome and acts as an energy generating machine in their cells.

"The PINK1 gene encodes the PINK1 protein, and one of the mutations leads to lower levels of mitochondria in the mitochondria," said Professor Verstreken. "Surprisingly, blocking FASN, which is not limited to mitochondria, actually avoids the PINK1 mutant mitochondria effect, thus blocking FASN increases the amount of specific type of lipid in the mitochondria and reduces the degradation of neurons.

Professor Verstreken has identified several goals for future research projects seeking a deeper understanding of the linkages between specific levels of lipid in neurons and Parkinson's disease. "Before developing new treatments, we need to answer questions such as "whether there is a link between early Parkinson's prevalence and progress and lipid content, "Professor Verstreken said. “Although we have successfully demonstrated that cardiolipin can improve the function of mitochondria in flies, mouse models and human cells, we still need to explore its effect on actual patients." By the way, Flarebio provides you with high-quality recombinant proteins including recombinant TLR2 for your research.

To prevent and treat cancer cachexia with MEK inhibitor

Tumor cachexia is a multifactorial syndrome characterized by progressive skeletal muscle atrophy and weight loss, and this condition can’t be fully reversed by conventional nutritional support, leading to progressive organ dysfunction. Cachexia not only reduces the sensitivity of drug treatment and increases the incidence of complications, affecting the implementation of patients with comprehensive treatment programs, but also leads to decreased quality of life and survival of patients significantly to be reduced. Clinically, with the lack of cachexia drugs with effective prevention and treatment, new ideas based on the understanding of the new breakthrough of pathogenesis in the treatment of cachexia have been the hot spots in domestic and foreign research in recent years. More research through recombinant mouse proteins is needed.

Skeletal muscle atrophy is the most important clinical features of cachexia. Clinical and basic research has always been taking skeletal muscle atrophy as a prognostic indicator of clinical cancer patients with reduced quality of life and shortening life expectancy. When the weight of the cachexia was 30%, the reserve of skeletal muscle protein decreased by 75% and the survival time was significantly shortened. The journal Cell reported that the quality of animal skeletal muscle was not only able to effectively reverse the decline in cachexia and significantly prolong the survival of model animals without affecting the rate of tumor growth. These results suggest that slowing the cachexia skeletal muscle atrophy is an important goal of its prevention and treatment. But there is no clinical intervention in the current cachexia skeletal muscle atrophy drugs.

MEK / ERK signaling pathway is not only important in tumor cell proliferation and differentiation, but also in regulating skeletal muscle energy metabolism and protein synthesis. A clinical study of advanced cholangiocarcinoma showed that the specific adverse effect of the first generation MEK inhibitor siMedidine was an increase in skeletal muscle mass, but the mechanism was unknown. To this end, the animal experimental results of Dr. Yang Quanjun from Shanghai Jiaotong University Affiliated Sixth People's Hospital Guo Cheng Task Force showed that the preventive and therapeutic administration of sixtemidine can effectively prevent and interfere with tumor cachexia animal weight and skeletal muscle, and it also can reduce the expression of E3 ubiquitination ligase MuRF1 and MAFbx (skeletal muscle protein degradation mainly by the two ubiquitin ligated ligands) and reduce the food intake and serum cytokines. Further studies on MyHC and MEK / ERK-related signaling pathways in the gastrocnemius muscle showed that siemetilib could inhibit the activation of ERK and increase the phosphorylation of AKT, leading to a decrease in the phosphorylation of FoXO3α and GSK3β downstream and increase of phosphorylation of mTOR.

The results of the Gregory B. Lesinski team from the Winship Cancer Institute in Emory University show that the second-generation MEK inhibitor, Binimetinib, also increases skeletal muscle mass and the function is gained through promoting skeletal muscle fibers synthesis and inhibition of skeletal muscle protein ubiquitination degradation. These results suggest that antineoplastic MEK inhibitors may be used for the prophylaxis and treatment of certain advanced stages of the disease in the future. By the way, Flarebio provides you with superior recombinant proteins including recombinant ITGB5 at good prices.

SPOP: new treatment target for renal cancer

In recent years, the incidence of renal cancer increased the rate of malignant tumors in the first place. Clinical treatment shows that renal cancer is not sensitive to radiotherapy and chemotherapy. VEGFR inhibitors such as sorafenib and sunitinib are the first-line drugs for advanced renal cell carcinoma. Although FDA-approved drugs for kidney cancer treatment has been up to ten, these drugs are very limited efficacy of metastatic renal cell carcinoma, and susceptible to drug resistance. According to previous research using recombinant mouse proteins, it is a very important and urgent task to discover and confirm the new drug targets for the treatment of RCC-specifics.

Liu Jiang, a researcher at the Beijing Genomics Institute of the Chinese Academy of Sciences, discovered early that the SPP of the ubiquitin ligase E3 family member Cul3-binding substrate protein was overexpressed in 99% of clear-cell renal cell carcinoma tissues and was expressed in normal renal tissue SPOP and is still a biomarker of clear cell renal cell carcinoma. SPOP is still overexpressed in metastatic clear cell renal carcinoma. Liu Jiang group further study showed that SPOP is incorrectly positioned in the cytoplasm cell renal cell carcinoma. Overexpression of hypoxia-inducible factor HIF transcription enhances SPOP overexpression and hypoxic microenvironment drives the accumulation of overexpressed SPOP proteins in the cytoplasm of renal carcinoma and ultimately promotes the formation of renal carcinoma.

The above fundamental research in biology poses a key scientific question whether small molecule compounds can targetly interfere with SPOP-mediated protein interactions to achieve specific treatment of clear cell renal cell carcinoma. In order to study the interaction between SPOP and protein, SPROP was used to identify the crystal structure of the substrate polypeptide complex, and the structure-based screening strategy was used in combination with drug Chemical synthesis optimization and other technical means. The successful acquisition of SPOP can be combined with small molecule compounds. The compound can inhibit the binding of SPOP to substrate protein, interfering with the SPOP-mediated regulation of ubiquitination of PTEN, DUSP7 and other ubiquitination-modified signal transduction pathway, and ultimately inhibiting the growth of clear cell renal carcinoma cells in vitro and in vivo. This important result is published in the journal Cancer Cell. This study provides evidence for the pharmacological function of SPOP as a target for clear-cell renal cell carcinoma, as well as a new direction for the discovery of SPOP inhibitors and for the treatment of renal cell carcinoma, unlike kinase inhibitors. Almost at the same time, Nature has published two reports on the hypoxia-inducible factor HIF-2α inhibitor PT2399 (analogue PT2385 has entered the clinical stage), suggesting that the HIF pathway for the Small molecule inhibitors will also become a new target for renal cancer treatment. Flarebio offers recombinant proteins of good quality such as recombinant Itgb2 for your research.

A new leap forward the prevention and treatment of fatty liver treatment

Researchers from the Institute of Biomedical Sciences (Barcelona Biomedical Research Institute) and IDIBAPS Biomedical Research Institute published their research using recombinant mouse proteins in the journal Nature Cell Biology. The researchers hope that this discovery will lead to a new leap forward the prevention and treatment of fatty liver treatment. One of the co-leaders of the study, IDIBAPS group leader Dr. Mercedes Fernández, said that it laid a good foundation for subsequent applied sciences.

Fatty liver is caused by depletion of CPEB4 in mice, and no one knows exactly what causes fatty liver, although we do know that people who are obese or overweight, or those with diabetes, high cholesterol or high triglycerides are more likely to suffer from fatty liver. In addition, rapid weight loss and poor eating habits can also lead to fatty liver. However, NAFLD may also occur in some populations without these risk factors.

Dr. Fernández and his colleagues noted that some large genomics studies have found that gene variants that encode CPEB4 are associated with dyslipidemia. In their study, the murine liver of CPEB4 was lowly expressed in the study. They found that with age, mice gradually developed fatty liver. They also found that feeding a high-fat diet to young mice deficient in CPEB4 resulted in a more pronounced fatty liver.

Further studies on the expression of CPEB4 at the molecular level suggest that this protein plays a key role in the liver stress response. For example, placing a liver cell in a stressful state caused by a high-fat diet can disturb the balance of a cell component called endoplasmic reticulum (ER). When lacking for CPEB4, ER shows less response on the stress. ER has many functions, including the production of protein and lipid and the removal of excess waste.

The researchers found that ER regains its balance by releasing CPEB4 to adapt to stress - for example, removing excess waste. They also found that circadian rhythms affected the release of CPEB4; it was more active during the day (the liver had a lot of work to do) and was quietest at night. The team believes that without CPEB4, ER can not fully restore the balance of stress, which will lead to fat accumulation, forming fatty liver. Flarebio offers high-quality recombinant proteins like recombinant TLR2 for your research.

New technology can track antitumor immune cells

The immunotherapy of using human immune cells to attack cancer cells is the current international scientific research focus, but how specific immune cells in-vivo action has always been a mystery. US researchers have recently developed a new method using recombinant mouse proteins for the first time to achieve the body's immune cell location and surveillance.

At this stage, immunotherapy still has its limitations. The effect of immune cells to find and kill cancer cells sometimes is better than conventional cancer therapy, but sometimes it does not work. Doctors often have to wait a few months to check whether the tumor shrinks to know whether the immune cells attack cancer cells. If immunotherapy does not work, then the cancer cells may have spread or become more difficult to deal with.

Researchers at Stanford University and other researchers said in the online version of the US academic journal Science Translational Medicine that they spent 10 years to find a way to track immune cells.

They have genetically engineered immune cells from patients and added a "reporter gene", a gene that directs the synthesis of a protein that can be detected by positron emission tomography. After injecting genetically-modified immune cells back to the human body, we can know the location of immune cells, the number of information by detecting the relevant proteins to analyse whether they are close to the tumor and attack.

The researchers successfully tested this technique in glioblastoma patients. New technologies can also be used to track immune cells against other cancers.

"The technique, which can show how the living body's immune system works without removing any human tissue, is unprecedented," says professor Sanjff Gambier at Stanford University who led the study.

He introduced, "Immune cell imaging technology also brings a windfall. In one patient's test, some immune cells arrived in the tumor region of the patient's brain, but some of the immune cells went to another region of the brain, where a positron emission tomography revealed a second tumor that had not previously been found."

The researchers said that this can locate the immune cells to see whether it attacks cancer cells and help doctors to assess the effectiveness of immunotherapy for cancer patients and analyze its causes. Flarebio offers high-quality recombinant proteins including recombinant ECE1.

A new method to treat patients with hereditary immunodeficiency

Scientists have developed a new approach using recombinant mouse proteins to repair the defective gene in hematopoietic stem cells in patients with hereditary immunodeficiency - X-linked chronic granulomatous disease (X-CGD), according to foreign media reports. Scientists transplanted stem cells into mice that had been repaired and developed into white blood cells with normal function, demonstrating that they could be used to treat patients with X-CGD disease.

X-CGD is a hereditary disease with limited therapeutic options. It is caused by mutations in the CYBB gene, which can cause NOX2 protein deficiency and damage the ability of leukocytes to resist infection. X-CGD patients in vivo white blood cells can‘t kill bacteria, so they are susceptible to infection, threatening the safety of life. In the latest study, scientists from the National Institute of Allergy and Infectious Diseases (NIAID) under the National Institutes of Health focused on mutations in the CYBB gene in which a single change in the genetic code resulted in loss of activity of the NOX2 protein.

The researchers isolated hematopoietic stem cells from two patients and used a gene-editing technique, CRISPR-Cas9, to target and repair this mutant gene. This targeted gene repair method can be defective CYBB gene sequence back to normal human sequences. It is difficult to distinguish between correct genes and normal genes. In the process, the researchers didn't detect CRISPR-Cas9 gene editing technology to produce any unexpected effect. In contrast, other methods of restoring the function of mutated genes often lead to additional changes, including genetic material additions or losses.

The researchers also transplanted stem cells from X-CGD patients into immunodeficient mice and found that these stem cells did not produce adverse effects and that they could differentiate into leukocytes and produce functional NOX2 for up to five months. The study published in the journal Science Translational Medicine suggests that although they need further research, they are now able to provide a theoretical demonstration that this gene-editing method can repair hematopoietic stem cell gene mutations caused by some minor ailments.

Scientists are planning to carry out the next step. The ultimate goal is to use this method for X-CGD patients in clinical treatment. At the same time, they also said that this gene editing method is also applicable to other blood diseases caused by single gene mutation, such as sickle cell anemia. By the way, Flarebio provides you with good-quality recombinant proteins like recombinant CDH2 at good prices.

The dual life of cancer protein Dab2

According to research using recombinant mouse proteins, sometimes proteins play more roles than we expect. For example, Dab2 has been considered to be associated with cancer. This molecule is associated with a series of signaling proteins called the Ras-MAPK pathway. In many cancers, the components of Ras-MAPK mutate and begin to tell cells to grow out of control.

Dr. Xiang Xi Xu (Michael), a professor of cell biology at the University of Miami's Miller School of Medicine, discovered the Dab2 protein more than 20 years ago and has been studying its relationship with cancer since that time, according to researchers at the Sylvester Comprehensive Cancer Center in the United States. But now he has found that Dab2 has always been very low-key secret - it may have an important public health impact on the fight against obesity. In a study published in Scientific Reports, Xu's lab found that young mice without Dab2 did not experience weight gain when ingesting too much food. "These mice look normal and everything seems good unless we give them a high-fat diet," Xu said. "They just do not get fat."

The underlying mechanism may be around adipose-derived stem cells: immature cells, which can be split into more stem cells or differentiated into mature adipocytes. In normal mice, Dab2 inhibits Ras-MAPK, which in turn promotes a protein called PPA R. It helps in the differentiation of adipose-derived stem cells into mature adipocytes. Eliminating Dab2 can shorten this process.

Normal mice fed a high-calorie diet gained weight, knocking out Dab2 to keep mice slim - but only temporarily. As the mice mature, the metabolic effects dissipate. At six months, the Dab2 deletion had little effect. Xu believes that this is because mice (and humans) lose fat stem cells at maturity. This early impact may help to explain "why early weight problems may persist into adulthood and why many adults are so difficult to lose weight".

"Dab2 controls a group of adipose-derived stem cells that are slowly disappearing," says Xu. "It appears that children are particularly susceptible to eating, and they may increase the number of adipocytes and fat cells at a young age, and they can still make fat later in life. But the existing fat cells are growing, and childhood habits may affect adults, making them more prone to obesity.

From a public health perspective, these findings may reinforce the importance of "guiding children away from high-fat diets". This role of Dab2 has been identified and may lead to new drug strategies to combat childhood obesity as the protein may be an attractive target for drug development. By the way, Flarebio provides you with high-quality recombinant proteins including recombinant CDH2 for your research.

This microprotein existing in P-body is also vital to our body

In the genome of human body, there is a large number of genes small open reading frame (smORF). They encode too small proteins that most of these genes have not been annotated, not to mention the function of the protein they translate. These "microproteins" are difficult to detect. Therefore, scientists at Yale University and the Salk Institute have adopted a set of special methods through recombinant mouse proteins. They first cleared the larger volume of protein in the cell and then analyzed the amino acid sequence of the remaining protein components using liquid chromatography-mass spectroscopy proteomics and designed the biology Information algorithm. The results identified more than 400 such microproteins and their genes. The results have been published in the recent issue of the journal Nature.

Among the microproteins over 400, the scientists have performed a functional study of a protein that is involved in mRNA degradation in the cell and recycling excess mRNA, preventing mRNA from continuing to produce specific proteins that are no longer needed. Thus, the process of gene expression in the cell regulation is very important. However, for this mechanism, we didn't know that there is a "little" protein which plays a key role.

The protein, called Nobody, is indeed "obscure" as its name looks like. However, Nobody's actual full name is non-annotated P-body dissociating polypeptide, which means "un-annotated P-body dissociation polypeptide" and has high evolutionary conservatism.

The researchers found that Nobody exists in the P-body and has interaction with a variety of protein components (such as cap enzyme). P-body is consisting of mRNA and a variety of proteins, and it completes the mRNA degradation recovery process in the first step - dacapping. Experiments show that the level of Nobody in the cell is negatively correlated with the number of P-bodies, and abnormal changes in Nobody level would interfere with the normal mRNA recovery process.

"Although Nobody has not yet been associated with any specific disease, other micro-proteins have this potential," said Alan Saghatelian, professor of communication at the Salk Institute and one of authors of the paper. "For the search and analysis of these proteins, to reveal its role in physiological and pathological processes will be an exciting frontier in molecular biology." Flarebio offers high-quality recombinant proteins like recombinant NPP1 at competitive prices.