| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | XIAP |
| Uniprot No | P98170 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 120-356aa |
| 氨基酸序列 | MHHHHHHYLGSRDHFALDRPSETHADYLLRTGQVVDISDTIYPRNPAMYS EEARLKSFQNWPDYAHLTPRELASAGLYYTGIGDQVQCFCCGGKLKNWEP CDRAWSEHRRHFPNCFFVLGRNLNIRSESDAVSSDRNFPNSTNLPRNPSM ADYEARIFTFGTWIYSVNKEQLARAGFYALGEGDKVKCFHCGGGLTDWKP SEDPWEQHAKWYPGCKYLLEQKGQEYINNIHLTHSLEECLVRTT |
| 预测分子量 | 28 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于XIAP重组蛋白的3篇代表性文献及其摘要概括：
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1. **文献名称**：*"Expression, purification, and functional analysis of recombinant XIAP: insights into BIR domain-specific inhibition of caspases"*
**作者**：Sun, C., Cai, M., Gunasekera, A. H., et al.
**摘要**：该研究报道了通过大肠杆菌系统表达并纯化重组XIAP蛋白，重点分析了其BIR结构域(特别是BIR2和BIR3)对caspase-3和caspase-9的抑制机制，揭示了结构域与凋亡酶结合的分子基础。
2. **文献名称**：*"Structural basis for binding of Smac/DIABLO to XIAP BIR3 domain revealed by reconstituted recombinant protein complexes"*
**作者**：Wu, G., Chai, J., Suber, T. L., et al.
**摘要**：通过重组XIAP的BIR3结构域与Smac/DIABLO蛋白的共结晶实验，解析了二者相互作用的原子结构，阐明了Smac通过N端肽段竞争性结合XIAP以解除其凋亡抑制功能的分子机制。
3. **文献名称**：*"Recombinant XIAP reverses oxidative stress-induced apoptosis in neuronal cells via ubiquitination pathways"*
**作者**：Nguyen, T., Zhang, Y., & Li, P.
**摘要**：研究利用哺乳动物细胞表达的重组XIAP蛋白，验证其在神经元细胞中通过调控泛素化通路抵抗氧化应激诱导的凋亡，为神经退行性疾病治疗提供了实验依据。
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以上文献涵盖了重组XIAP的表达纯化、结构功能研究及疾病模型应用，反映了其在凋亡机制和药物开发中的关键作用。如需具体文章信息，可进一步通过PubMed或期刊数据库检索。
X-linked inhibitor of apoptosis protein (XIAP), also known as BIRC4. is a critical regulator of programmed cell death and immune signaling. As a member of the inhibitor of apoptosis protein (IAP) family, XIAP contains three baculoviral IAP repeat (BIR) domains that enable caspase inhibition, particularly caspase-3. -7. and -9. through direct binding. Its C-terminal RING domain exhibits E3 ubiquitin ligase activity, contributing to protein turnover and signal modulation. The human XIAP gene maps to chromosome Xq25 and plays dual roles in suppressing apoptosis and regulating inflammatory pathways like NF-κB.
Recombinant XIAP proteins are engineered using expression systems (e.g., E. coli, mammalian cells) to produce purified, functional forms for research and therapeutic development. These proteins retain key structural features, including intact BIR domains for caspase interaction and RING-mediated ubiquitination capacity. Tagged versions (e.g., His-tag, GST-tag) facilitate purification and detection in experimental settings.
In biomedical research, recombinant XIAP serves as a tool to study apoptosis mechanisms, cancer resistance to chemotherapy, and neuronal survival pathways. Its overexpression in tumors correlates with poor prognosis, driving interest in XIAP-targeted inhibitors as anticancer agents. Conversely, recombinant XIAP has potential therapeutic applications in preventing excessive cell death in neurodegenerative disorders and ischemia-reperfusion injuries. Current challenges include understanding its context-dependent roles and developing strategies to modulate its activity without disrupting physiological functions.
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