Neurology Diagnostics

Archive for the ‘Antibody’ Category

COX IV isoform 1 is a nuclear-encoded polypeptide chain of the cytochrome c oxidase enzyme, located on the mitochondrial inner membrane. Owing to its widespread distribution in human and mammalian tissues, COX IV antibodies are widely used as loading controls for immunological assays. However, following pioneering research done by Wang et al in 1996, the COX IV antibody catalog has also proven useful in the areas of hypoxia, apoptosis and cancer research.

Cytochrome c oxidase is the terminal enzyme of the electron transport chain in the mitochondrion. Its function is to couple electrons transferred from reduced cytochrome C to molecular oxygen, contributing to a proton electrochemical gradient in the process. The COX complex in composed of 13 mitochondrial-encoded and nuclear-encoded subunits. The mitochondrial subunits are known to regulate electron transfer and the proton pump. While the function of the nuclear-coded subunits is less clear, they are thought to be involved with regulating the assembly of the complex.

Research has revealed cytochrome c plays an important role in apoptosis. Following apoptotic stimulation, Bcl-2 triggers caspase release, causing a change in mitochondrial permeability. This in turn initiates the release of COX, which binds to Apaf-1 in combination with dATP (deoxyadenosine triphosphate) to form the apoptosome complex, activating procaspase-9 and triggering the apoptosis cascade. In 2010, Yuan et al. were able to identify the roles of COX and dATP in great detail, using electron cryomicroscopy and single-particle technology.

We at Novus Biologicals have an extensive range of COX IV antibodies, proteins, lysates and RNAi products in our antibody catalog.

PMRT antibodies are widely used in protein regulation studies. The PMRT family of enzymes catalyse arginine methylation, a post-translational, irreversible modification affecting the activity of many key proteins.

Our antibody catalog has antibodies to all seven PMRT proteins so far discovered. They have been shown to play an essential regulatory role in many fundamental protein pathways, methylating histones, nuclear factors, cell cycle proteins, signal transduction proteins, enhancer binding factors, apoptosis proteins and viruses.

Arginine methylation is defined as the covalent tagging of methyl groups to protein arginine residues. This can regulate proteins activity or promote recognition by binding partners. This process is catalysed by distinct PRMT enzymes, in association with various cellular subunits, with methylation reactions occurring at N and C termini and the side chains of various amino acid residues, in particular the modification of arginine side chain guanidine groups. Arginine methylation shows reversible covalent modification similar to dephosphorylation; however the extent to which demethylation occurs is currently unknown.

The distinct chemical interactions generated by arginine methylation modifications are key to many regulatory protein pathways, and in recent years it has become clear that the process is as important as phosphorylation in controlling protein function. PMRT Antibody studies have shown arginine methylation plays a functional role in mRNA splicing, signal transduction, transcriptional control, DNA repair and protein translocation.

Recently, M. Yanovsky and A. Kornblihtt, of the Howard Hughes Medical Institute, Venezuela, found PMRT5 to be a key regulatory protein in animal and plant circadian rhythms, conserved in the evolution of both plants and insects. We at Novus Biologicals have a large PRMT antibody database, including several PRMT5 antibodies which are used in circadian studies, cell cycle studies and chromatin research.

People often think our products cover the entire genome, i.e. the DNA information contained in all the chromosomes. This would make ours a very unwieldy antibody catalog indeed, since the human genome alone covers some 3 billion DNA base pairs! What they really mean is the exome, that part of the genetic blueprint which responsible for encoding proteins and synthesising genes and functional genetic products. Called exons, these genes comprise just 1.5% of the human genome – yet are responsible for 85% of all diseases, and are at the heart of our antibody database.

DNA sequencing, i.e. the deciphering of DNA bases, is the key to protein research. However, before deciding what genes to target and which antibodies to use, clinical researchers first have to sift through thousands of hard-to-interpret non-coding sequences. This whole-genome method is both time consuming and costly.

Recently, disease researchers have been using new methods of sequencing that avoid the whole-genome approach, instead focussing on specific areas of the genome of interest to their area, i.e. the exome. Called exome capture, it specifically targets this area of the human genome, in particular the exons (around 180,000 in all) most likely to have disease-linked mutations. Some researchers fine-tuned this further still. One study was limited to X chromosome exons, while another targeted both coding and noncoding sequences of 21 genes specific to cancer.

Exome capture is both time and cost effective. Most researchers aren’t interested in the entire genome, and are often unable to interpret the non-coding sequence variants within the sample anyway. Their aim is to fit as many useful antibody assays into the available time-frame as possible.