caspase 3 antibody

Cell death via apoptosis is a basic cellular function occurring through the cell death receptor family and their ligands which signal through downstream adaptor molecules and the caspase protease family. Caspases have a precursor form composed of a prodomain, and large and small catalytic subunit, and are activated through a cleavage adjacent to an aspartate to liberate units and allow formation of an a2b2 tetramer. Caspase 3 is a cytoplasmic caspase with two isoforms (one acts as a dominant negative inhibitor), and is involved in the activation cascade for apoptosis execution.

Caspase 9 (also termed ICE-LAP6, Mch6, Apaf-3) is a member of cysteine protease family of caspases and is encoded by the CASP9 gene in humans. Caspase-9 is involved in mitochondrial apoptosis pathway and is an initiator caspase.

Caspase 7 (also known as CASP7, Mch3, ICE-LAP3, CMH-1) is a member of caspase family of cysteine proteases. It is an apoptosis-related cystein peptidase encoded by the CASP7 gene in humans. CASP7 homologous sequences have been identified in nearly all mammals. Similar to Caspase 3, Caspase-7 is an effector caspase and plays a key role in apoptotic execution.

Apoptosis is one of the best-characterized phenomena in cellular and molecular biology. Not only is it essential for successful development, but its deregulation also leads to a number of human diseases, most notably cancer.

S100A6 antibodies detect a small calcium binding protein with 2 EF-hand structures and belongs to the S100 family. Calcium binding induces a conformational change of the protein which in turn permits its interaction with several target proteins. It is predominantly expressed in fibroblasts and epithelial cells and has been implicated in several cellular processes such as cell cycle progression, cytoskeleton rearrangement and exocytosis.

Heat Shock Proteins (HSPs) are a ubiquitous group of molecular chaperone proteins that have evolved unique mechanisms, within their host cells, to facilitate survival in hostile environments such as heat, oxidative (hypoxia), pH and cold.

The caspases are a group of cysteine protease enzymes essential to apoptosis, inflammation and necrosis. Caspase 3 has been identified as one of the key mediators of apoptosis.

The PARP (Poly(ADP-ribose) polymerase) protein is a zinc-dependant nuclear enzyme whose main role is to detect and repair DNA single-strand breaks (SSB). However, PARP antibody research has revealed there are at least 17 PARP proteins, which also play a major role in apoptosis (programmed cell death) and post-translational modification. We at Novus Biologicals have an extensive range of PARP antibody products in our antibody catalogu.

Caspase 3 is a member of the cysteine-aspartic acid protease family and an important mediator of apoptosis. Caspase 3 antibody reagents have been used in cancer, Alzheimer's disease and stem cell research. A recent caspase 3 antibody ELISA study showed elevated levels of the p17 caspase 3 fragment were associated with myocardial infarction in humans.

Various studies have been performed tracking the involvement of p38 mitogen-activated protein kinase (MAPK) and caspase-3 antibodies in cobalt chloride (CoCl2) induced apoptosis in PC12 cells.

Studies have proven the usefulness of CoCl2 treatment to induce apoptosis in PC12 rat tumor cells. Treating these cells with CoCl2 leads to programmed cell death (apoptosis). Such cells provide a simple and useful model for the study of hypoxia-related neuronal disorders, as hypoxia involves a lack of oxygen.