Anti-cIAP-1/HIAP-2

cIAP1 (HIAP2, MIHB)is a member of the family of inhibitor of apoptosis proteins (IAP). Resistance towards apoptosis is a hallmark of cancer cells, and overexpression of IAPs can contribute to the development of cancer though inhibiting apoptosis.The IAPs, including cIAP1, have widespread tissue protein expression, with expression levels and subcellular localization patterns differing depending on the cell lineage. This antibody recognizes human cIAP1 is a 618 amino acid protein. In addition to at least one BIR domain, some IAP members also have a RING-type finger motif at their carboxyl-terminal. The RING finger domain of several IAPs, including cIAP2, have E3 ubiquitin ligase activity and target the degradation of Smac/DIABLO through ubqiuitination. Smac/DIABLO is a death inducer and functions by inhibiting IAP-caspase interactions, thereby promoting apoptosis. Degradation of cell death inducers like Smac/DIABLO is thought to be a conserved mechanism by which IAPs enhance their anti-apoptotic activity, thereby promoting cell survival. Protein function: Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, mitogenic kinase signaling, and cell proliferation, as well as cell invasion and metastasis. Acts as an E3 ubiquitin- protein ligase regulating NF-kappa-B signaling and regulates both canonical and non-canonical NF-kappa-B signaling by acting in opposite directions: acts as a positive regulator of the canonical pathway and suppresses constitutive activation of non-canonical NF-kappa-B signaling. The target proteins for its E3 ubiquitin- protein ligase activity include: RIPK1, RIPK2, RIPK3, RIPK4, CASP3, CASP7, CASP8, TRAF2, DIABLO/SMAC, MAP3K14/NIK, MAP3K5/ASK1, IKBKG/NEMO, IKBKE and MXD1/MAD1. Can also function as an E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway, targeting effector caspases for neddylation and inactivation. Acts as an important regulator of innate immune signaling via regulation of Toll-like receptors (TLRs), Nodlike receptors (NLRs) and RIG-I like receptors (RLRs), collectively referred to as pattern recognition receptors (PRRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase- dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8. Can stimulate the transcriptional activity of E2F1. Plays a role in the modulation of the cell cycle. [The UniProt Consortium]