| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | BCL2L1 |
| Uniprot No | Q07817 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-209aa |
| 氨基酸序列 | MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEGTESEMETPSAINGNPSWHLADSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIAAWMATYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQER |
| 预测分子量 | 39.4kDa |
| 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BCL2L1(Bcl-xL)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**: "Structure of Bcl-xL-Bak peptide complex: Recognition between regulators of apoptosis"
**作者**: Sattler M, et al.
**摘要**: 该研究通过X射线晶体学解析了BCL2L1(Bcl-xL)与促凋亡蛋白Bak的BH3结构域复合物的三维结构，揭示了Bcl-xL通过疏水相互作用结合Bak以抑制细胞凋亡的分子机制。
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2. **文献名称**: "BH3-only proteins trigger cytochrome c release, primarily by permeabilizing mitochondrial outer membranes"
**作者**: Kuwana T, et al.
**摘要**: 本文利用重组Bcl-xL蛋白，证明其通过与BH3-only蛋白(如Bid)的相互作用调控线粒体外膜通透性，进而影响细胞色素c的释放和细胞凋亡进程。
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3. **文献名称**: "An inhibitor of Bcl-2 family proteins induces regression of solid tumours"
**作者**: Oltersdorf T, et al.
**摘要**: 研究报道了一种靶向Bcl-xL等抗凋亡蛋白的小分子抑制剂ABT-737.通过重组蛋白实验验证其对Bcl-xL的结合能力，并展示其在肿瘤治疗中的潜在应用。
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4. **文献名称**: "Regulation of apoptosis by endoplasmic reticulum pathways"
**作者**: Germain M, et al.
**摘要**: 探讨了Bcl-xL在内质网应激中的调控作用，利用重组蛋白技术证实其通过抑制内质网相关Caspase激活来维持细胞存活。
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以上文献涵盖了结构生物学、功能机制及药物开发方向，均为BCL2L1研究领域的经典工作。
BCL2L1. also known as Bcl-xL, is a member of the Bcl-2 protein family that plays a central role in regulating mitochondrial apoptosis. Encoded by the BCL2L1 gene located on human chromosome 20 (20q11.21), this anti-apoptotic protein functions by binding and neutralizing pro-apoptotic family members like Bax and Bak, thereby preventing cytochrome c release and caspase activation. Its expression is critical for cell survival under stress conditions and is tightly regulated through alternative splicing, producing both anti-apoptotic (Bcl-xL) and pro-apoptotic (Bcl-xS) isoforms. Dysregulation of Bcl-xL is implicated in cancer progression, neurodegenerative diseases, and resistance to chemotherapy.
Recombinant BCL2L1 protein is engineered using expression systems (e.g., E. coli, mammalian cells) to produce purified, functional protein for research and therapeutic development. This recombinant form retains the conserved Bcl-2 homology (BH) domains required for interactions with apoptotic regulators. Structural studies using recombinant Bcl-xL have revealed its 3D architecture, including the hydrophobic groove critical for binding BH3-only proteins, facilitating drug discovery efforts. Small-molecule inhibitors like ABT-263 (navitoclax), designed to mimic BH3 domains, target this groove to reactivate apoptosis in cancer cells.
In biomedical research, recombinant BCL2L1 is widely used to study apoptosis mechanisms, screen anti-cancer compounds, and explore its dual roles in diseases. Overexpression in cancers correlates with poor prognosis, while its neuroprotective effects in Alzheimer’s or stroke models highlight context-dependent functions. Challenges remain in developing selective Bcl-xL inhibitors to minimize platelet toxicity, driving interest in isoform-specific therapies. Recombinant protein technology continues to advance our understanding of Bcl-xL’s pathophysiological roles and its potential as a therapeutic target.
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