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Kitul XIAP ELISA (uman) (OKCD00340)
XIAP ELISA Kit (Human) (OKCD00340)
4467.46 RON
În stoc
Număr Catalog 247-OKCD00340Description of target: 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 direct caspase inhibitor. Directly 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.12 Publications
 <p>Manually curated information for which there is published experimental evidence.</p>
 
 
 <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment iniRef.7"X-linked IAP is a direct inhibitor of cell-death proteases."_x005F_x005F_x000D_Deveraux Q.L., Takahashi R., Salvesen G.S., Reed J.C._x005F_x005F_x000D_Nature 388:300-304(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION.Ref.8"Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death."_x005F_x005F_x000D_Suzuki Y., Nakabayashi Y., Takahashi R._x005F_x005F_x000D_Proc. Natl. Acad. Sci. U.S.A. 98:8662-8667(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, MUTAGENESIS OF CYS-450.Ref.10"Proteasome-mediated degradation of Smac during apoptosis: XIAP promotes Smac ubiquitination in vitro."_x005F_x005F_x000D_MacFarlane M., Merrison W., Bratton S.B., Cohen G.M._x005F_x005F_x000D_J. Biol. Chem. 277:36611-36616(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION.Ref.12"A novel role for XIAP in copper homeostasis through regulation of MURR1."_x005F_x005F_x000D_Burstein E., Ganesh L., Dick R.D., van De Sluis B., Wilkinson J.C., Klomp L.W., Wijmenga C., Brewer G.J., Nabel G.J., Duckett C.S._x005F_x005F_x000D_EMBO J. 23:244-254(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH COMMD1, FUNCTION.Ref.14"Akt phosphorylation and stabilization of X-linked inhibitor of apoptosis protein (XIAP)."_x005F_x005F_x000D_Dan H.C., Sun M., Kaneko S., Feldman R.I., Nicosia S.V., Wang H.-G., Tsang B.K., Cheng J.Q._x005F_x005F_x000D_J. Biol. Chem. 279:5405-5412(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PHOSPHORYLATION AT SER-87, UBIQUITINATION, PROTEASOMAL DEGRADATION.Ref.20"Apoptosis-inducing factor is a target for ubiquitination through interaction with XIAP."_x005F_x005F_x000D_Wilkinson J.C., Wilkinson A.S., Galban S., Csomos R.A., Duckett C.S._x005F_x005F_x000D_Mol. Cell. Biol. 28:237-247(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, MUTAGENESIS OF HIS-467, INTERACTION WITH AIFM1.Ref.22"X-linked inhibitor of apoptosis protein (XIAP) regulates PTEN ubiquitination, content, and compartmentalization."_x005F_x005F_x000D_Van Themsche C., Leblanc V., Parent S., Asselin E._x005F_x005F_x000D_J. Biol. Chem. 284:20462-20466(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN THE UBIQUITINATION OF PTEN, INTERACTION WITH PTEN.Ref.26"Systematic in vivo RNAi analysis identifies IAPs as NEDD8-E3 ligases."_x005F_x005F_x000D_Broemer M., Tenev T., Rigbolt K.T., Hempel S., Blagoev B., Silke J., Ditzel M., Meier P._x005F_x005F_x000D_Mol. Cell 40:810-822(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE OF THE NEDD8 CONJUGATION PATHWAY.Ref.27"Regulation of the copper chaperone CCS by XIAP-mediated ubiquitination."_x005F_x005F_x000D_Brady G.F., Galban S., Liu X., Basrur V., Gitlin J.D., Elenitoba-Johnson K.S., Wilson T.E., Duckett C.S._x005F_x005F_x000D_Mol. Cell. Biol. 30:1923-1936(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN THE UBIQUITINATION OF CCS, INTERACTION WITH CCS.Ref.30"Nondegradative ubiquitination of apoptosis inducing factor (AIF) by X-linked inhibitor of apoptosis at a residue critical for AIF-mediated chromatin degradation."_x005F_x005F_x000D_Lewis E.M., Wilkinson A.S., Davis N.Y., Horita D.A., Wilkinson J.C._x005F_x005F_x000D_Biochemistry 50:11084-11096(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN THE UBIQUITINATION OF AIFM1.Ref.36"XIAP monoubiquitylates Groucho/TLE to promote canonical Wnt signaling."_x005F_x005F_x000D_Hanson A.J., Wallace H.A., Freeman T.J., Beauchamp R.D., Lee L.A., Lee E._x005F_x005F_x000D_Mol. Cell 45:619-628(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TLE3 AND TCF7L2/TCF4.Ref.44"XIAP induces NF-kappaB activation via the BIR1/TAB1 interaction and BIR1 dimerization."_x005F_x005F_x000D_Lu M., Lin S.-C., Huang Y., Kang Y.J., Rich R., Lo Y.-C., Myszka D., Han J., Wu H._x005F_x005F_x000D_Mol. Cell 26:689-702(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 10-99 IN COMPLEX WITH TAB1, FUNCTION, MUTAGENESIS OF TYR-75; VAL-80; VAL-86 AND LEU-98. ;Species reactivity: Human;Application: ELISA;Assay info: Assay Methodology: Quantitative Sandwich Immunoassay;Sensitivity: < 0.056 ng/mL
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