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Validated All-in-One™ qPCR Primer for BIRC3(NM_001165.4) Search again
Product ID:
HQP009084
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
AIP1, API2, CIAP2, HAIP1, HIAP1, IAP-1, MALT2, MIHC, RNF49, c-IAP2
Gene Description:
baculoviral IAP repeat containing 3
Target Gene Accession:
NM_001165.4(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.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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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. The encoded protein inhibits apoptosis induced by serum deprivation but does not affect apoptosis resulting from exposure to menadione, a potent inducer of free radicals. The amino acid sequence predicts three baculovirus IAP repeat domains and a ring finger domain. Transcript variants encoding the same isoform have been identified. [provided by RefSeq].
Gene References into function
- REVIEW: Genetic alterations involving API2 underlying the pathogenesis of MALT lymphoma
- promotes tumor cell survival in mesothelioma
- Interferon-beta therapy exerts a regulatory effect on peripheral T lymphocytes through an anti-apoptosis mechanism that involves the downregulation of cellular Inhibitor of Apoptosis Protein expression.
- These results indicate that IAPs alone are not the main factor responsible for the resistance of non-small-cell lung cancer cells to treatment.
- pathway and antiapoptotic effect of up-regulation of cIAP2 by G-CSF in neutrophils, and overexpression of cIAP2 in chronic neutrophilic leukemia
- Cellular inhibitors of apoptosis 1 and 2 are ubiquitin ligases for the apoptosis inducer Smac/DIABLO.
- Fuses with MALT1 and defines a distinctive clinicopathologic subtype in pulmonary extranodal marginal zone B-cell lymphoma of mucosa-associated lymphoid tissue.
- cIAP1 and cIAP2 are potential oncogenes and are overexpressed in multiple lung cancers with or without higher copy numbers
- these results indicate that unlike Smac/DIABLO, Omi/HtrA2's catalytic cleavage of IAPs is a key mechanism for it to irreversibly inactivate IAPs and promote apoptosis.
- cIAP-2 is an important regulator of apoptosis in bladder cancer and its overexpression may make tumours less susceptible to therapy involving apoptosis.
- overexpression of PKC delta induced cIAP-2 promoter activity and increased NF-kappa B transactivation, suggesting regulation of cIAP-2 expression by a PKC delta/NF-kappa B pathway
- copy numbers of API2-MALT1 do not reflect tumor cell proportions, and that the number of copies of API2-MALT1 in a tumor cell is different for each clinical sample.
- 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
- PR39 causes an increase in gene expression from a transfected human cDNA IAP-2 promoter in BAEC cells. PR39-induced increase in the level of IAP-2 mRNA in BAECs is due to an increase in transcription rate and mRNA stability.
- decreased cIAP2 may play a role in increased apoptosis in aged humans
- cAMP can induce c-IAP2 expression in colon cancer cells through CREB phosphorylation and CRE-dependent transcription in a manner that involves activation of ERK1/2 and p38 MAPK
- X-linked XIAP is present in Chronic lymphocytic leukemia cells and is up-regulated in conditions where apoptosis is prevented.
- Detection of API2-MALT1 fusion transcripts is useful for evaluating the prognosis and clinical behavior of the MALT lymphoma.
- NF-kappa B signaling, once activated in a CD40-dependent immune response, is maintained and enhanced through deregulation of MALT1 or formation of an API2-MALT1 fusion
- API2-MALT1 transcript was confirmed to be associated with the levels of apoptosis and API2 of MALT lymphoma.
- cIAP2 expression is up-regulated by IFN-alpha and IFN-gamma through the JAK2-STAT3 pathway, and increased expression of the cIAP2 protein may contribute to an IFN-alpha- and IFN-gamma-mediated antiapoptotic effect on human neutrophils.
- Upregulation of c-IAP2 by E6 and E7 may confer resistance to apoptosis that is necessary for sustained growth of some HPV16- and HPV18-positive cancer cells.
- Taken together, our results strongly indicated that API2-MALT1 possesses a novel mechanism of self-activation by up-regulating its own expression in t(11;18)(q21;q21)-carrying MALT lymphomas.
- IAP-2, XIAP, and survivin may make an important contribution to the resistance to the apoptotic effect of cisplatin in prostate cancer
- LPS and TNF-alpha, enhance monocytic cell survival through the induction of the antiapoptotic c-IAP2 gene in a human promonocytic THP-1 cell line.
- cIAP1 and cIAP2 bind but do not inhibit caspases
- demonstrates, for the first time, that BIRC3 (anti-apoptotic protein), COL3A1 (matrix protein synthesis), and CXCL3 (chemokine) were up-regulated in the thrombin-stimulated human umbilical vein endothelial cells
- Common translocation in MALT lymphoma results in a fusion of the cIAP2 region on chromosome 11q21 with the MALT1 gene on chromosome 18q21.
- cIAP2 is an inhibitor of antigenic signaling and implicate its dysfunction in MALT lymphomas.
- Tax-mediated HIAP-1 overexpression is required to suppress endogenous apoptosis and, therefore, is essential for the survival of HTLV-1-transformed lymphocytes
- Eosinophils of hypereosinophilic syndrome (HES) patients (but not normal eosinophils) express high levels of cellular IAP-2 (cIAP-2) and inhibit the caspase cascade in HES eosinophils.
- results reveal a physiological function of cIAP2, identify Bcl10 upregulation as a unifying molecular mechanism for MALT lymphomas, and define the mechanism and effects of this upregulation in t(11;18)-positive mucosa-associated lymphoid tissue lymphomas
- Detachment-induced upregulation of XIAP and cIAP2 delays anoikis of intestinal epithelial cells.
- Cell cycle-dependent G2/M-phase-specific cIAP2 expression is enhanced by NF-kappaB activation, and selective down-regulation of cIAP2 causes cells blocked in mitosis with nocodazole to become susceptible to apoptosis.
- the t(11, 18)(q21;q21) translocation creating the c-IAP2.MALT1 fusion protein activates NF-kappaB independently of TRAF1 AND TRAF2 and contributes to human malignancy in the absence of signaling adaptors that might otherwise regulate its activity
- Differential expression of IAPs in B-cell lymphomas suggests differences in pathogenesis that may have implications for novel treatment strategies targeting IAPs.
- Persistent infection of epithelial cell line with Chlamydophila pneumoniae resulted in the upregulation of the NF-kappaB regulated inhibitor of apoptosis protein 2 but not inhibitor of apoptosis protein 1 and apoptosis resistance.
- In particular, the stability of cIAP-2 is modulated by the presence of X-linked IAP and their interaction is stabilized in infected cells.
- TNF-alpha induced expression of c-IAP1 and c-IAP2 via MAP kinases, but not via NF-kappaB, and that MAP kinases participated in the inhibition of apoptosis by induction of c-IAPs in TNF-alpha-stimulated endothelial cells
- Trp323 of BIR3 plays a pivotal role both in maintaining necessary conformation for caspase-9 interaction and to a lesser extent, recognition of Smac-type peptide.
- Bortezomib inhibited expression of cIAP-1, cIAP-2, and XIAP, which are regulated by NF-kappaB and function as inhibitors of apoptosis.
- Levels of IAP-2 and Bax were decreased in A375 cells and HIF-1alpha was increased during hypoxia.
- Inflammation during active ulcerative colitis causes an upregulation of cIAP2 in regenerating epithelium, rendering the cells less susceptible to Fas ligation.
- Data show that Cartilage oligomeric matrix protein protects cells against death by elevating cIAP2 proteins.
- cIAP2 mRNA mediates translation only via ribosome bypassing 62 uAUGs. Shunting efficiency was altered by stress & was facilitated by a conserved RNA folding domain (1,470 to 1,877 nucleotides upstream) in a region not scanned by shunting ribosomes.
- The sequencing analysis of RT-PCR prducts confirmed the presence of the characteristic API2-MALT1 fusion transcript in patients with MALT lymphoma.
- XIAP and HIAP-1 in myelin lesions were co-localized with microglia and T cells 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.
- c-IAP1 and c-IAP2 are required for TNFalpha-stimulated RIP1 ubiquitination and NF-kappaB activation.
- IL-3 up-regulates the expression of the antiapoptotic proteins cIAP2, Mcl-1, and Bcl-X(L) and induces a rapid and sustained de novo expression of the serine/threonine kinase Pim1 that closely correlates with cytokine-enhanced survival.
- The ubiquitin-associated domain is required for XIAP and CIAP2-MALT1 to activate NF-kappaB.
- c-IAP2 is consistently overexpressed in nasopharyngeal carcinoma (NPC) cells; study reports that c-IAP2 plays a major role in the resistance of NPC cells to apoptosis induced by TLR3 stimulation
- cIAP1, cIAP2, and XIAP act cooperatively via nonredundant pathways to regulate genotoxic stress-induced nuclear factor-kappaB activation.