Recombinant Human E3 Ubiquitin-Protein Ligase Xiap (XIAP) Protein (His-SUMO)

Name: Recombinant Human E3 Ubiquitin-Protein Ligase Xiap (XIAP) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-09808P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human E3 Ubiquitin-Protein Ligase Xiap (XIAP) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P98170
Target Symbol	XIAP
Synonyms	AP 13; API3; Apoptosis Inhibitor 3; Baculoviral IAP repeat containing 4; Baculoviral IAP Repeat Containing Protein 4; Baculoviral IAP repeat-containing protein 4; BIRC 4; BIRC4; E3 ubiquitin-protein ligase XIAP; hIAP-3; hIAP3; HILP; IAP 3; IAP like protein; IAP-3; IAP-like protein; IAP3; ILP 1; ILP; ILP1; Inhibitor of apoptosis protein 3; Inhibitor of Apoptosis X Linked; Mammalian IAP Homologue A; MIHA; X linked IAP; X linked inhibitor of apoptosis; X linked inhibitor of apoptosis E3 ubiquitin protein ligase; X linked inhibitor of apoptosis protein; X-linked IAP; x-linked inhibitor of apopotosis proteins; X-linked inhibitor of apoptosis protein; Xiap; XIAP_HUMAN; XLP2
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MTFNSFEGSKTCVPADINKEEEFVEEFNRLKTFANFPSGSPVSASTLARAGFLYTGEGDTVRCFSCHAAVDRWQYGDSAVGRHRKVSPNCRFINGFYLENSATQSTNSGIQNGQYKVENYLGSRDHFALDRPSETHADYLLRTGQVVDISDTIYPRNPAMYSEEARLKSFQNWPDYAHLTPRELASAGLYYTGIGDQVQCFCCGGKLKNWEPCDRAWSEHRRHFPNCFFVLGRNLNIRSESDAVSSDRNFPNSTNLPRNPSMADYEARIFTFGTWIYSVNKEQLARAGFYALGEGDKVKCFHCGGGLTDWKPSEDPWEQHAKWYPGCKYLLEQKGQEYINNIHLTHSLEECLVRTTEKTPSLTRRIDDTIFQNPMVQEAIRMGFSFKDIKKIMEEKIQISGSNYKSLEVLVADLVNAQKDSMQDESSQTSLQKEISTEEQLRRLQEEKLCKICMDRNIAIVFVPCGHLVTCKQCAEAVDKCPMCYTVITFKQKIFMS
Expression Range	1-497aa
Protein Length	Full Length
Mol. Weight	72.7kDa
Research Area	Cancer
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	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.
Subcellular Location	Cytoplasm. Nucleus. Note=TLE3 promotes its nuclear localization.
Protein Families	IAP family
Database References	HGNC: 592 OMIM: 300079 KEGG: hsa:331 STRING: 9606.ENSP00000347858 UniGene: PMID: 28224479 Study identified the promoter region of miR-320a and verified three transcription factors, ATF2, ELK1, and YY1 to be responsible for inducing miR-320a expression under ionizing radiation conditions. Also, novel miR-320a target gene, XIAP, was identified. These findings suggest that miR-320a enhances the radiosensitivity of cancer cells. PMID: 30066913 Embelin promoted apoptosis via XIAP and PI3K/Akt signaling pathway. XIAP inhibitor Embelin inducing apoptosis could cause osteosarcoma cell death and inhibit its invasion. PMID: 30249882 prohibitin 1 regulates tumor cell apoptosis via the interaction with X-linked inhibitor of apoptosis protein PMID: 27025967 To expand the computational strategy designed when studying XIAP, we have applied the molecular modeling tools to a list of 140 variants seen in CFTR associated with cystic fibrosis, and a list of undiagnosed variants in 17 different genes. Graphical abstract XIAP in Caspase 3 and NOD2 signaling pathways. PMID: 28204942 A 3'UTR reporter assay confirms miR-124-3p to be a bona fide regulator of XIAP in CHO-K1 cells. This method demonstrates a useful approach to finding miRNA candidates for CHO cell engineering without competing for the cellular translational machinery. PMID: 28976632 The CASP-9 and -3/7 inhibitors XIAP 242Delta and Delta230 were prepared using the pGEX expression system and biochemically characterized. HtrA2 specifically binds to the BIR2 and BIR3 of XIAP at a 1:1 molecular ratio. in vitro cell-free CASP-9 and -3/7 Activation-apoptosis assays have demonstrated that these purified XIAP proteins dramatically inhibit CASP-9 and -3/7 action. PMID: 29631059 that XIAP rs8371 and rs9856 are associated with susceptibility to esophageal squamous cell carcinoma PMID: 29037837 In a systematic analysis of variants in 23 primary immuno-deficiencies-associated genes, study confirmed the association of variants in XIAP with Crohn's disease. PMID: 29501442 These results reveal that RPS3 upregulates XIAP independently of the NF-kappaB pathway in human breast cancer cells PMID: 29048653 downregulation of XIAP expression could enhance the sensitivity of RCC cells to apoptosis, and the basal expression of XIAP during apoptosis is stable. PMID: 29115633 XIAP promotes ubiquitylation and degradation of Bcl-2. PMID: 29020630 XIAP gene silencing would strengthen the radiosensitivity of esophageal cancer cells in vivo and in vitro, which provides a novel target for the treatment of esophageal cancer. PMID: 28821565 Findings of the study confirm that L-THP resulted in p53 independent apoptosis via down-regulating XIAP protein by inhibiting MDM2 associated with proteasome-dependent pathway and increased sensitivity of EU-4 cells against doxorubicin. PMID: 28721806 miR-23a induces trophoblast cell apoptosis by inhibiting XIAP, which may contribute to Preeclampsia. PMID: 28772220 These data suggest that XIAP may be playing an important role in the pathogenesis of breast cancer and can be therapeutically targeted either alone or in combination with PI3-kinase inhibition to induce efficient apoptosis in breast cancer cells. PMID: 28893228 loss of XIAP enhances filopodia formation in a Cdc42-dependent manner and this phenomenon phenocopies EGF stimulation. Further, XIAP depletion promotes lung colonization of tumor cells in mice in a Cdc42-dependent manner. These observations shed molecular insights into ubiquitin-dependent regulation of Cdc42 and that of actin cytoskeleton. PMID: 28661476 XIAP role in the cisplatin resistance in colon cancer PMID: 28667026 Here, the authors show that transcriptional regulator interacting with the PHD-bromodomain 1 (TRIP-Br1, Sertad1), a newly identified protein with poorly characterized functions, acts as an adaptor that bridges the interaction of multiple Adenylyl cyclase isoforms with X-linked inhibitor of apoptosis protein (XIAP), a RING-domain E3 ubiquitin ligase. PMID: 28656888 In gastroenteropancreatic neuroendocrine neoplasms survivin and XIAP regulate cell proliferation and apoptosis functioning as possible prognostic biomarkers and therapeutic targets. PMID: 28039474 A temporal succession of transcriptional and post-transcriptional regulatory mechanisms of the miR~23a~24-2~27a cluster, enabling a dynamic stress response and assuring cellular survival after radiation exposure by stabilizing XIAP. PMID: 28851536 the RING domain of XIAP has a role in promoting miR-4295 transcription, which reduces p63alpha translation and enhances urothelial transformation PMID: 27447744 These effects of metformin were accompanied by robust reductions in the protein levels of XIAP, a negative regulator of TRAIL-induced apoptosis. Silencing XIAP in TNBC cells mimicked the TRAIL-sensitizing effects of metformin. Metformin also enhanced the antitumor effects of TRAIL in a metastatic murine TNBC model PMID: 28324269 There were higher expressions of XIAP (p = 0.0032) and Bcl-2 (p = 0.0351) in the glioblastoma samples compared to the control samples of normal brain. These results raise the question of whether Bcl-2 and XIAP genes can be responsible for the inhibition of programmed cell death in glioblastomas. PMID: 29236891 These results show that significantly increased levels of FOXO3, IRF4, and xIAP mRNA in Chinese HIV-1-infected patients. PMID: 27841661 the aim of this review is to emphasize to clinicians that XIAP deficiency should be considered in patients suspected to have Crohn disease with early onset or an aggravated clinical course resistant to conventional therapy, and that appropriate treatment strategies are available. PMID: 27416006 uncovered a novel function of BIR domain of XIAP in regulating the EGFR translation PMID: 28057023 our study revealed a novel microRNA signaling pathway involved in cholangiocarcinoma and suggests that manipulation of the miR-410/XIAP pathway could have a therapeutic potential for cholangiocarcinoma PMID: 27259577 Inhibition of BET bromodomain-dependent XIAP and FLIP expression sensitizes KRAS-mutated non-small cell lung cancer to pro-apoptotic agents. PMID: 27607580 XIAP interacts with FAF1 and blocks FAF1-induced cell death. PMID: 28414080 The study identifies an unanticipated role for the X-linked inhibitor of apoptosis (XIAP) protein as a regulator of Lys63-linked polyubiquitination of HIF1alpha. PMID: 28666324 The authors find that primary human aggressive B-cell lymphoma samples exhibit high USP9X expression that correlate with XIAP overexpression. PMID: 27317434 Findings reveal important new insights into how XIAP 3'UTR works, suggesting that the non-coding XIAP 3'UTR serves as a competitor for miRNA binding and subsequently inactivates miRNA functions, by which XIAP 3'UTR frees the target mRNAs from being repressed. PMID: 28186968 XIAP is stable during mitotic arrest, but its function is controlled through phosphorylation by the mitotic kinase CDK1-cyclin-B1 at S40. PMID: 27927753 our findings suggest that X-linked inhibitor of apoptosis protein 3'-untranslated region serves as a competitive endogenous RNA for HMGA2 to activate hepatocellular carcinoma progression by arresting endogenous let-7a-5p. PMID: 28691642 In chronic myeloid leukemia cells, EZH2 modulates epigenetic changes at DNA methylated regions encoding miR-219 and downregulates the level of miR-219. Downregulation of miR-219 results in upregulation of XIAP and supports the survival of leukemia cells. PMID: 27070757 IFNgamma positively affects NOD2-mediated signaling in human conventional dendritic cells, in a manner considerably dependent on XIAP and partially dependent on mTOR. PMID: 26521691 miR-137 expression is inversely correlated with the level of XIAP protein in both ovarian cancer tissues and cell lines. these data suggest that multiple miRNAs can regulate XIAP via its 3'UTR. miR-137 can sensitise ovarian cancer cells to cisplatin-induced apoptosis, providing new insight into overcoming drug resistance in ovarian cancer PMID: 27875524 results of this work support the role of XIAP in mediating NOD2 signaling while reconciling the role of X-linked lymphoproliferative syndrome 2 and very-early-onset inflammatory bowel disease XIAP mutations in inflammatory cell death and provide a set of tools and framework to rapidly test newly discovered XIAP variants. PMID: 28404814 Using recombinant proteins, this study investigated the influence of survivin on the inhibition of caspase-9 by XIAP in vitro. With a fluorescence-based assay for the apoptosome-stimulated activity of caspase-9, the study shows that survivin has no effect on the inhibition of caspase-9 by XIAP, neither in the presence nor in the absence of Smac. PMID: 27865841 Study found a negative correlation between Smac and XIAP at the level of protein but not mRNA in non-small cell lung carcinoma (NSCLC) patients. Overexpressed XIAP could degrade through ubiquitination, the mature Smac inhibiting NSCLC apoptosis. PMID: 27498621 Combined triple actions of the TRAIL, the IAPs inhibitor, AT406, and the c-FLIP expression inhibitor, rocaglamide (ART), markedly improve TRAIL-induced apoptotic effects in most solid cancer cell lines through the activation of an extrinsic apoptosis pathway PMID: 27210546 we identified X-linked inhibitor of apoptosis protein (XIAP) as a direct target of miR-509-3p. PMID: 27697095 MiR-874 inhibits growth, increases apoptosis and enhances chemosensitivity in CRC cells by targeting XIAP. PMID: 27221209 Data show that X-linked inhibitor of apoptosis protein (XIAP) mRNA and protein expression increased, whereas XIAP-associated factor 1 (XAF1) mRNA and protein expression decreased with the growth of radiation dose and exposure time. PMID: 27048285 We demonstrated that, while depletion of XIAP attenuates cell transformation, elevated USP11 significantly promotes the tumor colony formation through stabilization of XIAP. PMID: 28040451 High XIAP expression is associated with ovarian cancer. PMID: 26779627 miR-24 plays an important role in regulating the cell survival of periodontal ligament cells through targeting XIAP. PMID: 27188727 Herein, CEUS imaging during cancer treatment played an important role in evaluating the therapeutic effects of XIAP siRNA ultrasound-responsive microbubble are a promising theranostic system for cancer gene therapy. PMID: 26733262 herefore targeting XIAP and NF-kappaB pathways simultaneously can be investigated in more detail to make use of embelin and celastrol as a combination therapy of cancer PMID: 27072230

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Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

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