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Validated All-in-One™ qPCR Primer for BIRC2(NM_001256163.1) Search again
Product ID:
HQP063663
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
API1, HIAP2, Hiap-2, MIHB, RNF48, c-IAP1, cIAP1
Gene Description:
baculoviral IAP repeat containing 2
Target Gene Accession:
NM_001256163.1(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Summary
The protein encoded by this gene is a member of a family of proteins that inhibits apoptosis by binding to tumor necrosis factor receptor-associated factors TRAF1 and TRAF2, probably by interfering with activation of ICE-like proteases. This encoded protein inhibits apoptosis induced by serum deprivation and menadione, a potent inducer of free radicals. [provided by RefSeq].
Gene References into function
- Expression of cIAP1, a target for 11q22 amplification, correlates with resistance of cervical cancers to radiotherapy.
- CD40 engagement enhances eosinophil survival through induction of cellular inhibitor of apoptosis protein 2 expression: implications for allergic inflammation
- Smac-penetratin fusion peptide crossed the cellular membrane, bound XIAP and cIAP1, displaced caspase-3 from cytoplasmic aggregates, and enhanced drug-induced caspase action in situ
- These results indicate that IAPs alone are not the main factor responsible for the resistance of non-small-cell lung cancer cells to treatment.
- Reovirus-induced apoptosis involves reduction of cellular IAP1 protein levels
- Cellular inhibitors of apoptosis 1 and 2 are ubiquitin ligases for the apoptosis inducer Smac/DIABLO.
- TRAF2, TRAF3, cIAP1, Smac, and lymphotoxin beta receptor associate and are involved in apoptosis
- c-IAP1 is an important intracellular modulator of Fas- as well as TNF-alpha death signalling pathways in human vascular smooth muscle cells.
- cIAP1 and cIAP2 are potential oncogenes and are overexpressed in multiple lung cancers with or without higher copy numbers
- although cIAP-1, cIAP-2 and XIAP transcripts were highly upregulated, their expression of endogenous proteins were not increased in HUVECs stimulated with LPS
- cIAP-1 has a role in regulating cell survival in endometrial cancer cells
- Relative risk of death was lower for cytoplasmic c-IAP1, cytoplasmic c-IAP2, and nuclear c-IAP2 expression. It was higher for nuclear c-IAP1 expression.
- levels of c-IAP1 and c-IAP2 are regulated by Smac/DIABLO through the ubiquitin/proteasome pathway
- HIAP2 is translationally induced during endoplasmic reticulum stress
- X-linked XIAP is present in Chronic lymphocytic leukemia cells and is up-regulated in conditions where apoptosis is prevented.
- c-IAP1 cellular location has a role in regulating cell differentiation
- No association of the TAP2 gene with schizophrenia in the Korean population.
- CIAP1 is downregulated and/or cleaved in a dose-dependent manner upon by anti-cancer drugs. cIAP-1's mitochondrial localization & liberation indicate a profoundly different function of this protein despite its similar modular structure to XIAP.
- expression in urethral epithelium upregulated by Neisseria gonorrhoeae PorB IB and upregulation dependent on NF-kappaB activation
- role for overexpressed cIAP1 in genetic instability, possibly by interfering with mitotic functions
- nuclear cIAP-1 expression appears to be a useful marker for predicting poor prognosis in head and neck squamous cell carcinoma (HNSCC), and may play roles in HNSCCs through the signaling pathway mediated by Smac/DIABLO and caspase-3
- There is endogenous cLAP1 expression in MKN45 cells, which may be a factor in the presumed anti-apoptotic system in these human gastric cancer cells.
- IAP1 protects neural progenitor cells against TRAIL-induced apoptosis and suppresses caspase-3 activation.
- a single cIAP can direct its E3 ligase activity toward different substrates and can alter the cellular functions of different protein targets, including TRAF2 and SMAC, in accordance with differences in the specificity of individual BIR domains
- cIAP1 and cIAP2 bind but do not inhibit caspases
- Since F-box proteins are specificity determining subunits of SCF ubiquitin protein ligases, our results suggest that Fbxo7 can mediate the ubiquitination of cIAP1 by SCF ubiquitin protein ligase and in the regulation of cIAP1 function.
- Results indicate a novel mechanism by which HIAP2 can regulate ER-initiated apoptosis by modulating the activity of caspase-2.
- High cIAP membranous expression is associated with epithelial ovarian cancer
- IAP family proteins may the prognosis of multiple myeloma patients in association with chemotherapy-induced overexpression of MDR1 or LRP.
- Differential expression of IAPs in B-cell lymphomas suggests differences in pathogenesis that may have implications for novel treatment strategies targeting IAPs.
- TNFR2 signaling induces selective c-IAP1-dependent ASK1 ubiquitination and terminates mitogen-activated protein kinase signaling
- Bortezomib inhibited expression of cIAP-1, cIAP-2, and XIAP, which are regulated by NF-kappaB and function as inhibitors of apoptosis.
- Importantly, our findings suggest that a paradox exists whereby Nrf2 activity is beneficial in non-malignant cells but in cancer cells it may provide a selective advantage for clonal expansion.
- Data show that Cartilage oligomeric matrix protein protects cells against death by elevating cIAP1 proteins.
- ME-BS directly interacts with the BIR3 domain of cIAP1, promotes auto-ubiquitylation dependent on its RING domain, and facilitates proteasomal degradation of cIAP1.
- Results suggest that HSP90 beta prevents auto-ubiquitination and degradation of its client protein c-IAP1, whose depletion would be sufficient to inhibit cell differentiation.
- the RING domain of cIAP1 mediates the degradation of RING-bearing inhibitor of apoptosis proteins by distinct pathways
- HIAP-1 and HIAP-2 mRNA levels were elevated in resting T cells while NAIP mRNA was increased in whole blood in multiple sclerosis
- cIAP1 and cIAP2 promote cancer cell survival by functioning as E3 ubiquitin ligases that maintain constitutive ubiquitination of the RIP1 adaptor protein.
- Nuclear, cytoplasmic and concurrent cIAP-1 immunoreactions were significantly correlated with lymph node metastasis in tongue squamous cell carcinomas.
- c-IAP1 and c-IAP2 are required for TNFalpha-stimulated RIP1 ubiquitination and NF-kappaB activation.
- once in the cytoplasm, cIAP1 is involved in the degradation of the adaptor protein tumor necrosis factor receptor-associated factor 2 (TRAF2) by the proteosomal machinery
- Inhibitor of Apoptosis Proteins 1 is an important member of the inhibitor of apoptosis family of proteins and is involved in the regulation of the NF-kappa B-signalling pathway downstream of the Tumor Necrosis Factor receptor.
- The ubiquitin-associated domain is essential for the oncogenic potential of cIAP1.
- cIAP1, cIAP2, and XIAP act cooperatively via nonredundant pathways to regulate genotoxic stress-induced nuclear factor-kappaB activation.