Apoptosis or programmed cell death is a fundamental cellular process that is essential for normal tissue development and abnormal growth such as cancer, neurodegeneration, autoimmune diseases, and angiogenesis, etc. Apoptosis is driven by two classes of specialized proteases known as caspases (Cysteine Aspartase). The initiator caspases can be activated by self-cleavage. The effector caspases are then activated in an amplification cascade. Mitochondria play a pivotal role in the regulation of apoptosis. Several key factors are released from the mitochondria that regulate apoptosis. The first such factor (Cytochrome-C) to be described binds to a cytoplasmic scaffolding protein called Apaf-1. Binding of the mitochondria factor allows Apaf-1 to form a ternary complex with, and activate, the initiator pro-caspase-9. Active caspase-9 then turns on downstream effector caspases, initiating apoptosis. Several key proteins regulate apoptosis by suppressing (e.g., Bcl-2 and related family of proteins) or promoting (e.g., AIF etc) apoptosis pathway. Bcl-XL is a known anti-apoptotic protein that acts at a late post-mitochondrial step. A new intracellular membrane protein, Aven (from Aventine, a Roman stronghold) has now been shown to bind both Bcl-XL and Apaf-1. Aven (mouse 342aa, human 362 aa) is a conserved protein that has broad tissue distribution with prominent expression in heart, skeletal muscle, kidney, liver, pancreas, testis, and several established cell lines (HeLa, IB4, and Raji). Aven interferes with the ability of Apaf-1 to self-associate, and subsequent inhibition of Apaf-1 mediated activation of caspases.
仕様
Size：100ug
Source Antigen：Mouse synthetic peptide
Grade：Highly Purified
Purity：Highly purified
Form：Supplied as a liquid in PBS, pH 7.2
Specificity：Mouse control peptide has no significant sequence homology with other proteins
