Recombinant ヒト XIAP protein (GST tag C-Terminus)
Recombinant Human XIAP protein (GST tag C-Terminus)
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Recombinant Human XIAP protein (GST tag C-Terminus) is a Human Full Length protein, in the 1 to 497 aa range, expressed in Baculovirus infected Sf9 cells, with >70%, suitable for SDS-PAGE, WB.
別名を表示する
API3, BIRC4, IAP3, XIAP, E3 ubiquitin-protein ligase XIAP, Baculoviral IAP repeat-containing protein 4, IAP-like protein, Inhibitor of apoptosis protein 3, RING-type E3 ubiquitin transferase XIAP, X-linked inhibitor of apoptosis protein, ILP, hILP, IAP-3, hIAP-3, hIAP3, X-linked IAP
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human XIAP protein (GST tag C-Terminus) (AB125537)
SDS-PAGE analysis of ab125537.
Reactivity data
配列情報
出荷温度及び保存条件
製品の状態
精製方法
出荷温度
短期保存温度
長期保存温度
分注に関する情報
保管に関する情報
補足情報
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
The function of XIAP involves regulation of apoptosis an important process in maintaining cellular homeostasis. It forms part of the apoptosome complex by interacting with caspases to prevent premature cell death. XIAP serves to protect cells from stress-induced apoptotic signals helping in survival under adverse conditions. This ability makes it a subject of interest in studying cancer survival mechanisms since overactive XIAP can allow cancer cells to avoid programmed cell death.
Pathways
Apoptosis regulation and cell survival pathways prominently feature XIAP. Particularly XIAP plays a role in the intrinsic apoptotic pathway which is activated in response to internal stress signals. XIAP regulates this pathway via its interaction with caspase-9 and interactions with other proteins such as Smac/DIABLO which can antagonize XIAP's function. This interaction is key in balancing cell death and survival therefore highlighting its role in apoptosis control.
一般的な情報
機能
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 (PubMed : 11257230, PubMed : 11257231, PubMed : 11447297, PubMed : 12121969, PubMed : 12620238, PubMed : 17560374, PubMed : 17967870, PubMed : 19473982, PubMed : 20154138, PubMed : 22103349, PubMed : 9230442). Acts as a direct caspase inhibitor (PubMed : 11257230, PubMed : 11257231, PubMed : 12620238). Directly bind to the active site pocket of CASP3 and CASP7 and obstructs substrate entry (PubMed : 11257230, PubMed : 11257231, PubMed : 16352606, PubMed : 16916640). Inactivates CASP9 by keeping it in a monomeric, inactive state (PubMed : 12620238). 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, RIPK2, MAP3K2/MEKK2, DIABLO/SMAC, AIFM1, CCS, PTEN and BIRC5/survivin (PubMed : 17560374, PubMed : 17967870, PubMed : 19473982, PubMed : 20154138, PubMed : 22103349, PubMed : 22607974, PubMed : 29452636, PubMed : 30026309). Acts as an important regulator of innate immunity by mediating 'Lys-63'-linked polyubiquitination of RIPK2 downstream of NOD1 and NOD2, thereby transforming RIPK2 into a scaffolding protein for downstream effectors, ultimately leading to activation of the NF-kappa-B and MAP kinases signaling (PubMed : 19667203, PubMed : 22607974, PubMed : 29452636, PubMed : 30026309). 'Lys-63'-linked polyubiquitination of RIPK2 also promotes recruitment of the LUBAC complex to RIPK2 (PubMed : 22607974, PubMed : 29452636). Regulates the BMP signaling pathway and the SMAD and MAP3K7/TAK1 dependent pathways leading to NF-kappa-B and JNK activation (PubMed : 17560374). Ubiquitination of CCS leads to enhancement of its chaperone activity toward its physiologic target, SOD1, rather than proteasomal degradation (PubMed : 20154138). Ubiquitination of MAP3K2/MEKK2 and AIFM1 does not lead to proteasomal degradation (PubMed : 17967870, PubMed : 22103349). Plays a role in copper homeostasis by ubiquitinating COMMD1 and promoting its proteasomal degradation (PubMed : 14685266). Can also function as E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway, targeting effector caspases for neddylation and inactivation (PubMed : 21145488). Ubiquitinates and therefore mediates the proteasomal degradation of BCL2 in response to apoptosis (PubMed : 29020630). 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 (PubMed : 22095281). Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8 (PubMed : 22095281). Acts as a positive regulator of Wnt signaling and ubiquitinates TLE1, TLE2, TLE3, TLE4 and AES (PubMed : 22304967). 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 (PubMed : 22304967).
配列の類似性
Belongs to the IAP family.
翻訳後修飾
S-Nitrosylation down-regulates its E3 ubiquitin-protein ligase activity.. Autoubiquitinated (PubMed:12747801). Ubiquitinated by TRIM32; leading to proteasomal degradation (PubMed:21628460).
細胞内局在性
Nucleus
ターゲットの情報
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