Anti-XIAP Antibody Picoband® Fluoro647 Conjugated

XIAP, also known as IAP3 or BIRC4, is a protein that stops apoptotic cell death. It is mapped to chromosome Xq25. This gene encodes a protein that belongs to a family of apoptotic suppressor proteins. Members of this family share a conserved motif termed, baculovirus IAP repeat, which is necessary for their anti-apoptotic function. This protein functions through binding to tumor necrosis factor receptor-associated factors TRAF1 and TRAF2 and inhibits apoptosis induced by menadione, a potent inducer of free radicals, and interleukin 1-beta converting enzyme. This protein also inhibits at least two members of the caspase family of cell-death proteases, caspase-3 and caspase-7. Mutations in this gene are the cause of X-linked lymphoproliferative syndrome. Alternate splicing results in multiple transcript variants.

E3 ubiquitin-protein ligase XIAP;6.3.2.-; Baculoviral IAP repeat-containing protein 4; IAP-like protein; ILP; hILP; Inhibitor of apoptosis protein 3; IAP-3; hIAP-3; hIAP3; X-linked inhibitor of apoptosis protein; X-linked IAP; XIAP; API3, BIRC4, IAP3

E.coli-derived human XIAP recombinant protein (Position: A15-V244) . Human XIAP shares 89.4% and 90.7% amino acid (aa) sequence identity with mouse and rat XIAP, respectively.

Apoptosis, Apoptotic Markers, Cancer, Caspases, Cell Biology, Cell Death, Intracellular, Invasion/Microenvironment, Metabolism, Metabolism Processes, Pathways and Processes, Receptors

Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, copper homeostasis, mitogenic kinase signaling, cell proliferation, as well as cell invasion and metastasis. Acts as a caspase inhibitor. ly bind to the active site pocket of CASP3 and CASP7 and obstructs substrate entry. Inactivates CASP9 by keeping it in a monomeric, inactive state. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and the target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, CASP3, CASP7, CASP8, CASP9, MAP3K2/MEKK2, DIABLO/SMAC, AIFM1, CCS and BIRC5/survivin. Ubiquitinion of CCS leads to enhancement of its chaperone activity toward its physiologic target, SOD1, rather than proteasomal degradation. Ubiquitinion of MAP3K2/MEKK2 and AIFM1 does not lead to proteasomal degradation. Plays a role in copper homeostasis by ubiquitinationg COMMD1 and promoting its proteasomal degradation. Can also function as E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway, targeting effector caspases for neddylation and inactivation. Regulates the BMP signaling pathway and the SMAD and MAP3K7/TAK1 dependent pathways leading to NF-kappa-B and JNK activation. Acts as an important regulator of innate immune signaling via regulation of Nodlike receptors (NLRs) . 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. Acts as a positive regulator of Wnt signaling and ubiquitinates TLE1, TLE2, TLE3, TLE4 and AES. Ubiquitination of TLE3 results in inhibition of its interaction with TCF7L2/TCF4 thereby allowing efficient recruitment and binding of the transcriptional coactivator beta- catenin to TCF7L2/TCF4 that is required to initiate a Wnt-specific transcriptional program. .

1. Cummins, J. M., Kohli, M., Rago, C., Kinzler, K. W., Vogelstein, B., Bunz, F.X-linked inhibitor of apoptosis protein (XIAP) is a nonredundant modulator of tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) -mediated apoptosis in human cancer cells.Cancer Res. 64: 3006-3008, 2004. 2. Deveraux, Q. L., Takahashi, R., Salvesen, G. S., Reed, J. C.X-linked IAP is a inhibitor of cell-death proteases.Nature 388: 300-304, 1997. 3. Kim, J., Park, J., Choi, S., Chi, S.-G., Mowbray, A. L., Jo, H., Park, H.X-linked inhibitor of apoptosis protein is an important regulator of vascular endothelial growth factor-dependent bovine aortic endothelial cell survival.Circ. Res. 102: 896-904, 2008.