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Validated All-in-One™ qPCR Primer for XIAP(NM_001204401.1) Search again
Product ID:
HQP066914
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
API3, BIRC4, IAP-3, ILP1, MIHA, XLP2, hIAP-3, hIAP3
Gene Description:
X-linked inhibitor of apoptosis
Target Gene Accession:
NM_001204401.1(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.
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 which inhibit apoptosis through binding to tumor necrosis factor receptor-associated factors TRAF1 and TRAF2. This protein inhibits apoptosis induced by menadione, a potent inducer of free radicals, and ICE. It also inhibits at least two members of the caspase family of cell-death proteases, caspase-3 and caspase-7. [provided by RefSeq].
Gene References into function
- genomic organization reported; a novel transcript homologous to BIRC4 and expressed solely in the testis was identified
- The anti-apoptotic activity of XIAP is retained upon mutation of both the caspase 3- and caspase 9-interacting sites.
- caspase 3-mediated focal adhesion kinase processing in human ovarian cancer cells: possible regulation by X-linked inhibitor of apoptosis protein
- ILPIP, a novel XIAP-interacting protein acts as a co-factor enhancing XIAP-mediated activation of JNK1 and the caspase-independent protection of XIAP against apoptosis
- XIAP has a role in degrading smac and protecting cells from mitochondial damage
- calpain-mediated XIAP degradation contributes to initiation of apoptosis in normal neutrophils and dysfunction of this regulatory pathway can lead to pathological neutrophil accumulation.
- 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
- 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 XIAP protein levels
- nuclear ribonucleoproteins C1 and C2 are part of the RNP complex that forms on XIAP IRES, the cellular levels of hnRNPC1 and -C2 parallel the activity of XIAP IRES and the overexpression of hnRNPC1-C2 specifically enhanced translation of XIAP IRES
- findings indicate that the levels of XIAP and Bcl-X(L) are regulated by distinct pathways during monocytic differentiation, and that upregulation of these proteins contributes to the increased longevity of cells in the monocytic lineage
- the overexpression of XIAP inhibits taxol-induced apoptosis through the decrease of caspase-3 activity and inhibition of the processing of pro-caspase-3.
- RING domain was essentially required for the proteasomal association of XIAP and for its ubiquitination.
- Expression of XIAP and downregulation of Fas-L are linked to chemoresistance in ovarian carcinoma cells and may represent one of the potential antiapoptotic mechanisms involved during this process.
- identification of ubiquitination sites
- identification as substrate for mitochondrial serine protease Omi/HtrA2
- although cIAP-1, cIAP-2 and XIAP transcripts were highly upregulated, their expression of endogenous proteins were not increased in HUVECs stimulated with LPS
- XIAP protein has a role in preventing apoptosis in human lung cancer cells
- cytokines regulate the expression of XIAP in leukemic cell lines and primary AML blasts
- role in relief of caspase inhibition mediated by Smac
- XIAP is regulated by Smac3, a Smac/DIABLO splicing variant
- XIAP is a principal inhibitor of apoptosis overexpressed in human hepatocellular carcinoma and that XIAP may be a potential target for gene therapy of human HCCs
- Grim promoted XIAP ubiquitination and degradation.
- XIAP is a new downstream target of Akt and a potentially important mediator of the effect of Akt on cell survival
- XIAP interacts with CHEK1 during mitosis.
- Data suggest that ARTS induces apoptosis by antagonizing IAPs, including XIAP.
- no difference was observed in XIAP expression between young and aged subjects.
- XIAP up-regulation requires nuclear factor kappa b and has a role in Cyr61-induced resistance to apoptosis in breast cancer cells
- x-linked inhibitor of apoptosis protein and survivin have roles in progression of childhood de novo acute myeloid leukemia
- role of antagonizing XIAP in induction of caspase-dependent cell death in concert with authocatalytic processing of HtrA2/Omi
- First evidence is provided that increased XIAP levels protect the neonatal brain of transgenic XIAP-overexpressing mice against hypoxia-ischemia.
- These data demonstrate that full-length X-linked inhibitor of apoptosis (XIAP) inhibits caspase activation required for mitochondrial amplification of death receptor signals.
- ERK suppresses stress-induced apoptosis downstream of mitochondrial alterations by maintaining XIAP levels and oxidants block this effect through activation of p38 and protein phosphatases
- XIAP-mediated inhibition of apoptosis has a role during progression of clear-cell clear cell renal carcinomas.XIAP expression is a new independent prognostic marker in this tumor type.
- Data indicate that phenylurea-based XIAP antagonists block interaction of downstream effector caspases with XIAP, thus inducing apoptosis of tumor cell lines through a caspase-dependent, Bcl-2/Bax-independent mechanism.
- In drug-induced apoptosis XIAP & its BIR3-RING cleavage product redistribute into large nuclear inclusions, implying a new unknown function of XIAP and its BIR3-RING fragment.
- Treatment with rottlerin downregulated the protein levels of survivin and X-chromosome-linked IAP (XIAP), two major caspase inhibitors.
- The XIAP expression was significantly lower in patients with favorable than intermediate or poor cytogenetics (n = 74; P < 0.05).
- XIAP binds directly to the active-site pockets of effector caspases
- Genetically modified human islets expressing XIAP are resistant to the negative effects of immunosuppressive drugs on insulin secretion and cell viability.
- XIAP functions as ubiquitin ligase toward mature caspase-9 and Smac to inhibit apoptosis.
- IAP-2, XIAP, and survivin may make an important contribution to the resistance to the apoptotic effect of cisplatin in prostate cancer
- downregulation of the XIAP or survivin enhances cell death by TRAIL and increases sensitivity against some chemotherapeutic agents in hepatocellular carcinoma cells
- XIAP expression in colorectal cancer is regulated by hepatocyte growth factor/C-met pathway via Akt signaling
- The ratio of XAF1(A) and XAF1C mRNA expression differs amongst the cell lines tested, suggesting differential mRNA stabilities and/or the existence of tissue- or cell type-specific splicing regulation.
- These data identify an important function of XIAP in cardiomyocytes and point to a striking similarity in the regulation of apoptosis in postmitotic cells.
- XIAP has a pivotal role in apoptosis deregulation in cancer [review]
- These data provide an unsuspected link between copper homeostasis and the regulation of cell death through XIAP and may contribute to the pathophysiology of copper toxicosis disorders.
- ALK7-induced apoptosis is at least in part through two Smad-dependent pathways, Bax/Bcl-2 and Xiap.
- Detachment-induced upregulation of XIAP and cIAP2 delays anoikis of intestinal epithelial cells.
- down-regulation of XIAP by RNA interference markedly enhanced the susceptibility of HL cells for CTL-mediated cytotoxicity
- We show here that alpha-fetoprotein cancels XIAP-mediated inhibition of endogenous active caspases in cytosolic lysates of tumor cells, as well as XIAP-induced blockage of active recombinant caspase 3 in a reconstituted cell-free system.
- A sharp XIAP concentration threshold separates conditions of efficient apoptosis execution and inhibition
- high levels of XIAP control caspase activation and substrate cleavage, and may promote apoptosis resistance and sublethal caspase activation in vivo
- These studies identify XIAP as a new substrate of Raf-1.
- data suggest that the sensitization to radiation results from NBS1-siRNA-mediated suppression of DNA repair and/ or X-ray-induced cell survival signaling pathways through NFKB and XIAP.
- Differential expression of IAPs in B-cell lymphomas suggests differences in pathogenesis that may have implications for novel treatment strategies targeting IAPs.
- XLX, a Xenopus laevis inhibitor of apoptosis (IAP) family member, exhibits characteristics typical of an IAP, such as caspase inhibition and autoubiquitylation.XLX is phosphorylated during meiosis by protein kinases of the MAPK and MPF pathways.
- Reviewing current knowledge of the caspase-inhibitory potential of the human IAPs shows that XIAP is probably the only bona fide caspase inhibitor.
- Deguelin has great potential for chemosensitization of XIAP and could represent a new therapeutic agent for treatment of breast cancer.
- These results implicate elevated XIAP levels caused by high basal NF-kappaB activity in TRAIL resistance and suggest that therapeutic strategies involving TRAIL can be abetted by inhibition of NF-kappaB and/or XIAP only in tumor cells.
- In particular, the stability of cIAP-2 is modulated by the presence of X-linked IAP and their interaction is stabilized in infected cells.
- by identifying an XLP immunodeficiency that is caused by mutations in XIAP, we show that XIAP is a potent regulator of lymphocyte homeostasis in vivo
- XIAP is overexpressed in pancreatic cancer and contributes to chemoresistance
- Definition of the consensus sequences of the motifs that interact with the three BIR domains in an unbiased manner.
- The ability of the wild-type XIAP BIR3 domain as well as its Trp323Ser variant in inhibition of human caspase-9, binding to AVPFVASLPN (SMAC-peptide), SMAC protein, and mature caspase-9 was investigated.
- cytoplasmic hnRNP A1 is a negative regulator of XIAP internal ribosome entry site (IRES)-dependent translation, indicating a novel function for the cytoplasmic form of this protein.
- Endogenously expressed XIAP bound active forms of both caspase-9 and caspase-3. However, downregulation of XIAP were unable to induce caspase-9 activity, indicating that it is not a major determinant in blocking caspase-9 in NSCLC cells.
- XIAP regulates IL-6 transcription via NF-kappaB in cooperation with AP1 and C/EBP-beta.
- Overexpression of X-linked inhibitor of apoptosis proteins is associated with pancreatic cancers
- XIAP is upregulated in mesothelioma effusions and peritoneal mesotheliomas, suggesting a prosurvival role in malignant mesothelioma cells.
- Results demonstrate that cleavage by caspase 3 does not activate caspase 9, but enhances apoptosis by alleviating XIAP inhibition of the apical caspase.
- Downregulation of either FLIP or XIAP but not Bcl-2 restored sensitivity of Colo320 cells to Apo2L/TRAIL.
- Preservation of XIAP proteins represents a key mechanism by which PGI2 protects endothelial cells from oxidant-induced apoptosis.
- An increased expression ratio of XIAP to XAF1 in combination with a disturbed expression of the XAF1 splice variants could be shown in gastric adenocarcinomas.
- XIAP and Survivin are not involved in the cytoprotective effect of HGF against antineoplastic agents.
- Early Kupffer cell survival, even in the presence of tumor necrosis factor (TNF)-alpha, during Pseudomonas aeruginosa strain PA103 infection is mediated by stabilization of XIAP.
- Inhibitor of apoptosis proteins, nuclear factor-kappa, Smac/DIABLO and apoptosis inducing factor were increased in colon cancer cells.
- XIAP is highly expressed in esophageal cancer and its downregulation by RNAi sensitizes esophageal carcinoma cell lines to chemotherapeutics
- XAF1 mediates Survivin down-regulation through a complex containing XIAP, supporting dual roles for XAF1 in apoptosis
- Bortezomib inhibited expression of cIAP-1, cIAP-2, and XIAP, which are regulated by NF-kappaB and function as inhibitors of apoptosis.
- XIAP was highly specific for papillary thyroid carcinomas among the thyroid neoplasms thus it may be a useful marker for differential diagnosis.
- Data report the crystal structure of XIAP and suggest that dimerization may be important for its action in TGF-beta and BMP signaling and the action of cIAP1 and cIAP2 in TNF receptor signaling.
- adhesion-dependent activation of the PI3K/Akt/XIAP pathway may be one of the factors involved in the CAM-DR of U937 cells.
- XIAP homotrimerizes via its C-terminal Ring domain, making its inhibitory activity toward caspase-3 more susceptible to Smac.
- Studies using reporter constructs and NF-kappaB Rel-A deficient mouse embryonic fibroblasts showed that NF-kappaB signaling is required for the induction of Sod2 by XIAP. XIAP also reduced oxidative stress in the PC6.3 cells.
- XIAP is expressed at higher levels in prostate cancers compared with matched normal tissues and may have a role in reducing risk of tumor recurrence
- Strong XIAP immunostaining differentiates malignant from benign and hyperplastic mesothelial cell populations.
- identify apoptosis-inducing factor as a new XIAP binding partner and indicate a role for XIAP in regulating cellular reactive oxygen species
- Data show levels of XIAP are significantly elevated in the COMP-expressing cells and down-regulation XIAP protein levels by small interfering RNAs blocks the ability of COMP to enhance survival.
- findings suggest that the potent apoptotic inhibitor XIAP may be a biomarker in head and neck SCCs.
- Ectopic expression of Par-4 decreases levels of XIAP protein in thapsigargin-treated cells, caused in part by XIAP protein instability & caspase activation. XIAP instability & Akt inactivation are important in cellular pathways affected by Par-4.
- These results indicate that Nulp1 plays a role in cell death control and may influence tumor growth.
- These results suggest that XIAP polymorphisms do not significantly affect susceptibility to lung cancer in Koreans.
- Altogether these results highlight an intertwined role for specific Akt isoforms and XIAP in chemoresistance of uterine cancer cells.
- the role of triptolide as a sensitizer to TRAIL-induced apoptosis in part by independent modulation of XIAP expression and p53 signaling.
- XIAP elevation may be correlated with increasing melanoma thickness and tumor progression.
- Anti-myeloma effect of homoharringtonine with concomitant targeting of the myeloma-promoting molecules, Mcl-1, XIAP, and beta-catenin
- XIAP expression appears to be useful for distinguishing atypical adenomatous hyperplasia from adenomatous hyperplasia of the lung
- Smac/DIABLO interacts in a similar way with both XIAP and survivin through its amino terminal residues.
- XIAP plays a putative in vivo role in counteracting TNFalpha-induced apoptosis in endometrial tumor cells.
- No defects were observed in the coding sequence of XIAP in a cohort of 30 hypogammaglobulinemic patients; X-linked lymphoproliferative syndrome caused by XIAP deficiency may be a very rare differential diagnosis in male patients with CVID.
- study provides evidence that during T cell proliferation the intracellular caspase inhibitor X-linked inhibitor-of-apoptosis protein (XIAP) interacts with caspases-3/-7, thereby blocking their full activation, substrate cleavage, and cell death
- A mitochondrial block and expression of XIAP lead to resistance to TRAIL-induced apoptosis during progression to metastasis of a colon carcinoma.
- XIAP and HIAP-1 in myelin lesions were co-localized with microglia and T cells in multiple sclerosis
- confirmed a protective role of XIAP upstream of mitochondrial permeabilisation during TRAIL-induced apoptosis
- The effect of XIAP inhibition and PPARgamma activation in colon cancer, was explored.
- These findings suggest that calpain inhibition delays neutrophil apoptosis via cyclic AMP-independent activation of PKA and PKA-mediated stabilization of Mcl-1 and XIAP.
- Important molecule in controlling hepatocellular carcinoma metastasis. XIAP can be a molecular target subject to intervention to reduce metastasis and recurrence.
- Through interaction with MEKK2, XIAP functions in an ubiquitin ligase dependent manner to evoke a second wave of NF-kappaB activation, resulting in the modulation of NF-kappaB target gene expression.
- anti-apoptotic functions of cFLIPs may be attributed to inhibit oxaliplatin-induced apoptosis through the sustained XIAP protein level and Akt activation.
- COMMD1 mutant which was unable to bind to XIAP demonstrated a complete loss of basal ubiquitination
- High expression of XIAP and low expression of XAF1 is associated with gastric adenocarcinomas.
- These results suggest that simultaneously targeting both FLIP and XIAP may prove useful in the treatment of cancers, particularly those in which the intrinsic mitochondrial apoptotic pathway has been compromised.
- A combination of XIAP inhibition plus TRAIL is a promising strategy to overcome apoptosis resistance of pancreatic cancer.
- The purpose of this study was to test the feasibility of immunocytochemically detecting markers that may be affected by therapy or are predictive of therapeutic responsiveness, including phosphohistone H1, XIAP and p63.
- analysis of 4-substituted azabicyclo[5.3.0]alkane smac mimetics and their binding to the BIR3 domain of XIAP
- XIAP knockdown using RNA interference enhanced drug sensitivity and decreased tumor formation in NOD/SCID mice
- These data show an unexpected role of XIAP and cellular-inhibitor of apoptosis proteins in the turnover of C-RAF protein, thereby modulating the MAPK signalling pathway and cell migration.
- cIAP1, cIAP2, and XIAP act cooperatively via nonredundant pathways to regulate genotoxic stress-induced nuclear factor-kappaB activation.