New antibody therapy of Alzheimer’s disease may come true someday

In study on degenerative nervous disease shows that an antibody therapy can reduce the light β- amyloid plaques in the brain of Alzheimer's patients. The study has been published in the British journal Nature this week. The study provides preclinical data and preliminary results of clinical trials in stageⅠ. Through research of recombinant proteins like recombinant dog proteins, it is found that both of them support to further develop the antibody for the treatment of Alzheimer's disease.

The gradual accumulation of β- amyloid proteins in the brain is a sign of of Alzheimer's disease. It is generally considered that β- amyloid-related toxicity triggers synaptic dysfunction and neurodegeneration, both of which can lead to Alzheimer's disease. However, clinical therapy targeted to β- amyloid proteins has always been unsuccessful currently.

This time, researcher Alfred Sang Duoke and colleagues from the famous American biotech company Biogen reported the development condition of human monoclonal antibody Aducanumab. The drug was developed by Biogen for treatment of Alzheimer's disease. It can be selectively directed to fight against β- amyloid proteins and is known as the "new hope to overcome Alzheimer's disease". Now, researchers say that in the genetically-modified mouse model, Aducanumab can enter the brain and dose dependently reduces soluble and insoluble β- amyloid proteins.

The authors also conducted a double-blind and randomized, placebo-controlled Phase Ⅰ clinical trial to evaluate the safety and tolerability showed by Alzheimer's patients after monthly injecting Aducanumab to patients with mild cognitive impairment or mild dementia and brain exist β- amyloid deposits. In one-year period, 165 patients were monthly injected placebo or Aducanumab. After 54 weeks of treatment, β- amyloid proteins in the brain of patients injected with Aducanumab significantly reduced. The higher the dose, the greater the decrease amplitude of plaque; while the brain of patients inhected with placebo showed no significant changes. During the research, 40 patients discontinued treatment, because 20 of them showed adverse reactions, including dose-dependent amyloid-related imaging abnormalities.

The authors conculded that demonstration that anti-β- amyloid therapy can delay cognitive decline will completely change the way of understanding, treatment and prevention of Alzheimer's disease. Flarebio provides you with high-quality recombinant proteins such as recombinant CDH12 at good prices.

British scientists have another viewpoint on cancer metastasis

Cancer metastasis is the process of cancer cells separating themselves from primary tumor and spreading to other parts of the body through the blood or lymphatic system. Once the cancer spreads, the treatment becomes more challenging. Chemotherapy, hormone therapy, radiation therapy and other therapies like recombinant human proteins can be successful in the treatment of some metastatic cancers, but for most metastatic cancers, the prognosis is poor.

Recently, early study of UK Queen Mary University of London (QMUL) found that cancer cells seem to depend on an unusual survival mechanism to spread throughout the body. This discovery could help to find a prevention and treatment method of metastasizing and secondary tumors in the future. The study is published in the journal Nature Communications. The researchers used mice and zebrafish to conduct research and tested the changes that occurred when cancer cells broke away from a tumor cell cluster. Researchers revealed an unknown survival mechanism of cancer cells in the past and found that a molecule called "integrins" may be the key through experiments using recombinant mouse proteins.

Integrins are proteins on the surface of cells, and they act with surrounding environment around the cells. Integrins are involved in "outside-in" and "inside-out" signaling and can help cancer cells be adhered to the surrounding environment. But the study found that when cancer metastasizes, integrins change to a new form of communication from adhesion function which is a signal "from within the inside". The integrins send signals within cells, which has never been found before.

The researchers found that an integrin called β1and another protein called c-Met paired up and went into the interior of the cell together with each other. These two proteins would enter in a specific site in the cell, and the role of this site is to degrade and recover cellular components. But in this case, the site is used for cell communication. These two proteins would send signals to other regions of the cell and trigger defense mechanisms of cell death in the transfer process.

Integrin inhibitor has been tested as a method for the treatment of cancer. Currently, the drug can targetedly act on the activity of integrin signaling on the surface of cancer cells. The researchers said this may explain why the efficacy of these drugs is so poor. A new strategy is to block integrin proteins from entering the cell. The researchers hope this viewpoint can help to design better treatments for cancer metastasis. Flarebio offers recombinant proteins of good quality including recombinant Nrg2 at reasonable prices.

New breakthrough has been made in the study of breast cancer targeted treatment

Dr. Xu Lingzhi and his research team from the Second Affiliated Hospital of Medical University in Dalian have made new achievements in the field of breast cancer stem cell properties and targeted therapy. The achievements describes the key regulating effect of p62 / SQSTM1-let-7a / b-MYC signaling pathway on breast cancer stem cell properties for the first time and indicates that signaling hub protein p62 / SQSTM1 can be an effective target for intervention, providing new thoughts for overcoming the recurrence, metastasis and drug resistance of breast cancer. Related research papers are recently published online in the journal Cancer Gene, which also publishes some other studies on recombinant human proteins.

Currently, the clinical treatment of breast cancer has been improved greatly, but the phenomenon of recurrence and drug resistance is becoming more serious. More and more evidence suggests that tumor stem cells are highly correlated with drug resistance, relapse and metastasis during tumor treatment. However, because of the dynamic evolution and high-degree heterogeneity of tumor stem cells, therapies aimed at cancer stem cells still lacks for effective targets and intervention mechanisms.

As a "signal hub" within the cell, p62 / SQSTM1 protein combines with a variety of signaling molecules through its own series of functional domains to be involved in the regulation of various signaling pathways. In the study, researchers took breast cancer as an example. By in-vitro and in-vivo animal experiments of cell lines, the researchers reveal the signaling protein p62 / SQSTM1 highly express in cancer stem cell enriched population for the first time, and it plays positive regulation role to "dry” character of tumor stem cells. Intervention of the expression of the gene can significantly reduce the "dry" character of tumor stem cells. The research team also found that the signaling protein p62 / SQSTM1 can promote mRNA stability after oncogene MYC transcription by reducing the expression of a small RNA-let-7a / b, thus mediating "dry" phenotype of tumor stem cells. Subsequent analysis of clinical samples further validated that the high expression of signaling protein p62 / SQSTM1 was negatively correlated with PFS and OS in breast cancer patients. Flarebio provides high-quality recombinant proteins such as recombinant CDH4 at good prices.

Get to learn more about the role of PARP in cardiovascular disease

Poly ADP-ribose polymerase (PARP) is a protein which is widely concerned in the field of cancer treatment in recent years, for it plays an important role in the DNA repair process. PARP activity lies in that it conducts ADP-ribosylation to its substrate proteins through NAD +. When DNA shows breakage, PARP is activated and then makes histone ADP at break sites ribosylated, prompting histone seperates itself from DNA molecule, thereby conducting combination before repairing proteins. The findings were obtained through recombinant rat proteins. On the other hand, because the rate of rapidly DNA breaks of cancer cells which separate rapidly is quite frequent, once PARP is inhibited, DNA damage can accumulate quickly in the cancer cells, ultimately leading to cell death.

However, the role of PARP is not limited to DNA repair, and its medicinal value is also not limited to this. Recently, scientists from the US Southwestern Medical Center have found a wide range of functions in the PARP gene transcriptional regulation and RNA processing, opening up a new direction for cancer therapy development. Their results were published in the recent issues of Science.

"This discovery changes our understanding of the function of PARP, which may open a new field of drug development," corresponding author of the article Professor W. Lee Kraus said.

To systematically analyze the intracellular function site of PARP, the researchers transformed PARP so that it can conduct ADP-ribosylation NAD + substrate proteins which are modified by acetylene group, thus the introduction of the ADP ethynyl cycloaddition reaction may occur with fluorescently labeled molecule with an azide group, thus marking and identifying a number of PARP in cells in vitro substrates, including a variety of proteins as well as sites on the chromosome.

The negative transcription elongation factor (NELF) attracted special attention of researchers. NELF is involved in the pause process of RNA transcription, and this is to ensure that there is enough intracellular ribonucleotide used for the mechanisms of transcription. Under normal circumstances, PARP will conduct ADP- ribosylation to NELF, thus sending the signal of sufficient supply to NELF so that transcription can proceed.

"We found that the modifications of PARP to NELF can alter open or closed state of the gene in breast cancer cells, thus affecting the biological state of a cell fundamentally," Professor W. Lee Kraus said, "This is a newly-discovered link." Flarebio offers recombinant proteins of good quality including http://www.cusabio.com/Transmembrane-Protein/Recombinant-Human-Integrin-beta-2ITGB2-11153649.html" title="http://www.cusabio.com/Transmembrane-Protein/Recombinant-Human-Integrin-beta-2ITGB2-11153649.html"recombinant ITGB2 at competitive prices.

New potential tool of tagging innocuous protein

As we know that proteins and peptides of various sizes and shapes have been used since the early 80s to tag proteins with many different purposes, ranging from affinity purification to fluorescence-based microscopic detection in whole organisms. However, tagging strategies used nowadays run the risk that the native function of the protein may be abolished or compromised by interactions with the tag.

A study using recombinant proteins like recombinant horse proteins published yesterday at Nature Methods proposes the use of two plant protein epitopes, named inntags, as the most innocuous and stable tagging tools in the study of physical and functional interactions of proteins.

The study is leaded by the Molecular Biology Institute of Barcelona and the Joint Programme for Computational Biology of the Institute for Research in Biomedicine (IRB Barcelona) and the Barcelona Supercomputing Center, and University of Barcelona. It has analyzed the available list of polypeptides with known 3D structure to identify among them the most suitable for tagging purposes. Researches have selected the smallest protein domains that still display strong structural determinants to act as antigens, do not generate solubility issues, do not compromise cell fitness and cause no detectable functional and localization effects when fused to other target proteins.

A large series of bioinformatics tools were first used to scan through the entire planet proteome to select those proteins which could have good tagging properties. After manual curation of the in silico results 12 tag candidates were tested in vivo, finding excellent or outstanding properties for all of them. Inntags maintain their integrity, stability, solubility in cell extracts, diffusional mobility and do not cause important functional perturbations that commonly used tags -such as MYC, FLAG or HA- do cause. Moreover, the tests have shown the applicability of Allergen Phl p2 and Heiven Isoform 2 in immunofluorescence and immunoprecipitation analysis of a series of proteins in mouse fibroblasts and hippocampal neurons.

Compared with commonly used tags, inntags are clearly more innocuous. They may be the tools of choice to perform proteome-wide interactome studies, in situ analysis of proteins at the single-molecule level or when the target protein does not offer an obvious functional assay. The tools are believed to open new possibilities for researchers in cellular biology. Flarebio provides superior recombinant proteins such as recombinant APP at competitive prices.

Cancer Specialist: a new drug-resistant mechanism of lung cancer cells has been found

A research team from Hokkaido University in Japan recently announced that they have successfully discovered the new mechanism of lung cancer cells resisting anti-cancer drugs by inhibiting immune cell activity. Related results obtained through recombinant mouse proteins have been published in the leading US journal Cancer Specialist.

The researchers found that the surroundings of cancer cells having drug resistance would gather a lot of macrophages which have the function of swallowing and destroying damaged tissues, while most of these macrophages are the types which have the ability of inhibiting the activity of other immune cells. The team members investigated the relation between induced proteins of these types of macrophages Lnterleukin-34 and lung cancer cells.

The researchers conducted a six-month joint culture of lung cancer cells and anti-cancer agents and compared the residual lung cancer cells with drug resistance and normal lung cancer cells. The research found that the average lung cancer cells would not secrete interleukin-34, while lung cancer cells with drug resistance will secrete a lot of interleukin-34. Drug-resistant lung cancer cells would make use of interleukin-34 to convert macrophages into the type which can inhibit immune cells activity, thereby improving their ability to survive.

The mice study demonstrated that inhibiting the activity of interleukin-34 can enhance the treatment effect of anti-cancer drugs to drug-resistant lung cancer cells. The researchers said the drug-resistant mechanism of lung cancer cells explored in this research is different to the currently-known mechanisms, which is of great importance for the development of new therapeutic drugs. Flarebio offers recombinant proteins of good quality including recombinant ECE1.

NRG1 protein can help to effectively treat Alzheimer's disease

According to news from RIA Novosti on August 25th, US neuroscientists made use of recombinant human proteins and found an upgraded brain protein - neuregulin 1 (NRG1) and this protein can effectively help to treat Alzheimer's disease.

It is generally throught that Alzheimer's disease is due to too much amyloid pathogenic substance called β-amyloid protein depositing inside neuron. Such β-amyloid protein is formed from β-amyloid precursor protein (APP) proteolysis. It is involved in repairing damaged proteins and can be combined with protein molecules. β-amyloid protein can lead to the emergence of amyloid plaques and death of nerve cells.

While scientists from the United States Institute of Biology Khajuraho Cambiasso Turk have recently discovered a protein having a clear function - neuregulin-1. The protein can’t only clear the protein plaques in the brain but also can slow down the formation of β - amyloid plaques.

Scientists conducted experients with mice suffering from Alzheimer's disease. They put a special virus containing neuregulin-1 proteins in brain of the lab mice. The purpose is to make the neuregulin-1 genes grow in mice. During the process of experiment, the scientists made the mice to look for exit, and then they observed whether neuregulin-1 proteins would improve the memory capacity of mice and make the protein plaques in their neurons decrease. Experiments show that the neuregulin-1 protein does improve the memory capacity of mice and remove β- amyloid protein plaques.

Currently, scientists still don't know the specific reasons for this phenomenon. But they believe that neuregulin-1 protein can promote to form another peptide - enkephalinase enzyme which can solubilize protein agglomerate. However, whether the fact is true remains to be verified through the results of recent experiments.

Besides, scientists also said that the main advantages of neuregulin protein is that it can move freely through the barrier between the brain and the rest of the body, thus it can be flexibly used to treat Alzheimer's disease. Flarebio offers recombinant proteins of good quality such as recombinant EXT2.