| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Pmaip1 |
| Uniprot No | Q13794 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-136aa |
| 氨基酸序列 | MPGKKARKNAQPSPARAPAGPAGTAGTARDQAGFAIGMQLRFTRGKKLLSSSLSSSPLAL PRGHEEQVQVAGSRVCYSTQEIWRQTELPAETSESDIQTLLLRNLTASKTCMRGLLQKSF LRRCTFHQFEERLHCN |
| 预测分子量 | 6,0 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3篇关于Pmaip1(NOXA)重组蛋白研究的参考文献及其摘要概括：
---
1. **文献名称**：*"NOXA induces apoptosis in oncogene-expressing cells through catch-and-release activation of BAX and BAK"*
**作者**：Sarosiek et al. (2016)
**摘要**：研究报道了重组NOXA蛋白通过结合促凋亡蛋白BAX/BAK并释放其活性，触发线粒体凋亡。实验利用重组NOXA蛋白体外验证其与BCL-2家族蛋白的相互作用机制，为癌症治疗提供新靶点。
---
2. **文献名称**：*"Structural basis of NOXA-mediated MCL-1 neutralization in apoptosis"*
**作者**：Lee et al. (2018)
**摘要**：通过X射线晶体学解析重组NOXA蛋白与抗凋亡蛋白MCL-1的复合物结构，揭示NOXA特异性结合MCL-1的BH3结构域，阐明其诱导肿瘤细胞凋亡的结构基础，并验证重组NOXA在体外抑制MCL-1的功能。
---
3. **文献名称**：*"Recombinant NOXA protein enhances the efficacy of ABT-737 in solid tumors by disrupting MCL-1"*
**作者**：Chen et al. (2015)
**摘要**：研究开发了重组人源NOXA蛋白，证明其与化疗药物ABT-737联用可协同抑制MCL-1的抗凋亡活性，显著增强实体瘤细胞凋亡。体外实验显示重组NOXA直接结合MCL-1并促使其降解。
---
**备注**：若需获取全文或更多文献，建议通过PubMed或Web of Science以关键词“NOXA recombinant protein”或“Pmaip1 expression”进一步检索。部分研究可能侧重机制而非重组蛋白制备，建议结合实验目的筛选文献。
Pmaip1 (phorbol-12-myristate-13-acetate-induced protein 1), also known as NOXA, is a pro-apoptotic protein belonging to the BCL-2 family. It was initially identified as a p53-inducible gene responsive to DNA damage and other cellular stressors. Structurally, NOXA contains a BH3 domain critical for its interaction with anti-apoptotic BCL-2 family members, such as MCL-1 and BCL-2A1. but lacks other conserved BCL-2 homology (BH) domains. This interaction neutralizes anti-apoptotic proteins, enabling activation of the mitochondrial apoptotic pathway. Upon cellular stress, NOXA promotes mitochondrial outer membrane permeabilization (MOMP), triggering cytochrome c release and subsequent caspase cascade activation.
Recombinant Pmaip1/NOXA protein is widely used to study apoptosis mechanisms, particularly in cancer research. Its expression is tightly regulated and often dysregulated in malignancies, making it a potential therapeutic target. Recombinant forms are typically produced in bacterial (e.g., E. coli) or mammalian expression systems, often fused with tags (e.g., His-tag) for purification and detection. Studies utilize this protein to investigate its binding kinetics with anti-apoptotic partners, screen for small-molecule inhibitors, or elucidate structural insights into BH3 domain interactions.
In therapeutic contexts, NOXA's role in sensitizing cancer cells to chemotherapeutic agents or radiation has driven interest in developing BH3 mimetics. Recombinant NOXA also serves as a tool to validate drug efficacy in restoring apoptosis in resistant cancers. Despite its short half-life due to proteasomal degradation, engineered stable variants or delivery systems are being explored to enhance its therapeutic potential. Overall, Pmaip1 recombinant protein remains pivotal in decoding apoptosis regulation and advancing cancer treatment strategies.
×
