| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TRIAP1 |
| Uniprot No | O43715 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-76aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMNSVGEA CTDMKREYDQ CFNRWFAEKF LKGDSSGDPC TDLFKRYQQC VQKAIKEKEI PIEGLEFMGH GKEKPENSS |
| 预测分子量 | 11 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TRIAP1重组蛋白的假设性参考文献示例(仅供参考，实际文献需通过学术数据库查询)：
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1. **文献名称**：*"Recombinant TRIAP1 protein inhibits apoptosis in colorectal cancer cells"*
**作者**：Smith J, et al.
**摘要**：研究通过表达重组TRIAP1蛋白，发现其能显著抑制结直肠癌细胞凋亡，机制涉及阻断线粒体途径的caspase激活，并与化疗耐药性相关。
2. **文献名称**：*"Expression and purification of human TRIAP1 in E. coli for structural studies"*
**作者**：Lee S, et al.
**摘要**：报道了一种高效的大肠杆菌表达系统，用于生产可溶性重组人TRIAP1蛋白，并通过Ni柱亲和层析纯化，为后续结构生物学研究奠定基础。
3. **文献名称**：*"TRIAP1 recombinant protein modulates mitochondrial membrane stability in vitro"*
**作者**：Garcia R, et al.
**摘要**：体外实验表明，重组TRIAP1蛋白通过与HSPA9相互作用，稳定线粒体膜结构，减少细胞色素C释放，从而抑制内在凋亡通路。
4. **文献名称**：*"Functional characterization of TRIAP1 variants using recombinant protein assays"*
**作者**：Chen L, et al.
**摘要**：利用重组蛋白技术分析TRIAP1突变体的功能，发现某些癌症相关突变会削弱其抗凋亡活性，提示其在肿瘤发生中的潜在作用。
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**建议**：如需真实文献，可通过PubMed、Google Scholar等平台搜索关键词“TRIAP1 recombinant”“TP53-regulated inhibitor of apoptosis 1 protein”或结合具体研究方向(如癌症、凋亡机制)。
**Background of TRIAP1 Recombinant Protein**
TRIAP1 (TP53-regulated inhibitor of apoptosis 1), also known as p53CSV, is a small, evolutionarily conserved protein encoded by the *TRIAP1* gene. It was initially identified as a transcriptional target of the tumor suppressor protein p53. which plays a central role in regulating cell cycle arrest, DNA repair, and apoptosis in response to cellular stress. Unlike many p53-induced pro-apoptotic genes, TRIAP1 functions as an anti-apoptotic factor, specifically inhibiting the intrinsic (mitochondrial) pathway of apoptosis. It achieves this by interacting with HSPA9 (mortalin), a chaperone protein involved in mitochondrial function, thereby blocking the assembly of the apoptosome and subsequent caspase activation.
TRIAP1’s role in apoptosis suppression has linked it to cancer biology, particularly in contexts where tumor cells evade cell death to promote survival. Overexpression of TRIAP1 has been observed in certain cancers, correlating with poor prognosis and resistance to chemotherapy. Conversely, its downregulation sensitizes cancer cells to apoptosis, highlighting its potential as a therapeutic target. Beyond oncology, TRIAP1 is implicated in developmental processes and cellular stress responses, though its mechanisms remain under active investigation.
Recombinant TRIAP1 protein, produced via heterologous expression systems (e.g., *E. coli* or mammalian cells), retains the functional properties of the native protein. It is widely used in biochemical and cellular studies to dissect its anti-apoptotic activity, protein-protein interactions, and structural features. Researchers employ it in assays such as apoptosome formation inhibition, mitochondrial function analyses, and screening for small-molecule inhibitors. The availability of recombinant TRIAP1 facilitates mechanistic insights into apoptosis regulation and supports drug discovery efforts aimed at modulating its activity in disease contexts. Its study continues to advance understanding of cell survival pathways and their exploitation in pathologies.
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