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. Caspase-1 (interleukin-1 converting enzyme (ICE)) is a cytoplasmic protease that converts 34kD inactive precursor IL-1 to the mature 17kD proinflammatory cytokine. Caspase-1 is synthesized as a single-chain polypeptide zymogen consisting of an N-terminal prodomain, and a large (p20) and a small (p10) catalytic domains. A serine/threonine kinase RIP2/CARDIAK/RICK binds caspase-1 and promotes its processing. RIP2 engages caspase-1 through a direct protein-protein interaction involving corresponding caspase recruitment domains (CARDs) present at the C terminus of RIP2 and within the prodomain of caspase-1. It is now shown that activation of caspase-1 is regulated by a small CARD-containing decoy molecule termed ICEBERG. This decoy protein binds the corresponding CARD motif of caspase-1, inhibiting and/or displacing the upstream activator RIP2. Structurally, ICEBERG has resemblance to the death-domain-fold superfamily. Human Iceberg is a 90-aa protein (11q21-q22). It is 52% identical to the caspase-1 CARD. It is primarily expressed in the heart and placenta. The related CARD-containing molecules caspase-1 and RIP2 are also expressed in the heart and placenta as well as in numerous other tissues.
仕様
Size：100ug
Source Antigen：Human synthetic peptide
Grade：Highly Purified
Purity：Highly purified
Form：Supplied as a liquid in PBS, pH 7.2
Specificity：Peptide has no significant sequence homology with other proteins
