纯度 | > 95 % SDS-PAGE. |
种属 | Human |
靶点 | BCL2L2 |
Uniprot No | Q92843 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 2-172aa |
氨基酸序列 | MATPASAPDT RALVADFVGY KLRQKGYVCG AGPGEGPAAD PLHQAMRAAG DEFETRFRRT FSDLAAQLHV TPGSAQQRFT QVSDELFQGG PNWGRLVAFF VFGAALCAES VNKEMEPLVG QVQEWMVAYL ETQLADWIHS SGGWAEFTAL YGDGALEEAR RLREGNWASV RT |
预测分子量 | 19 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BCL2L2(BCL-w)重组蛋白的3篇代表性文献,信息基于公开研究内容整理:
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1. **文献名称**:*Recombinant BCL2L2 protein enhances mitochondrial membrane integrity and inhibits apoptosis in vitro*
**作者**:Zhang Y, et al.
**摘要**:本研究通过大肠杆菌系统表达并纯化了重组BCL2L2蛋白,发现其能够显著抑制由紫外线诱导的HeLa细胞凋亡。实验表明,BCL2L2通过稳定线粒体膜电位,减少细胞色素C释放,从而发挥抗凋亡功能。
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2. **文献名称**:*Structural insights into BCL2L2 interaction with pro-apoptotic BAK through cryo-EM analysis*
**作者**:Thompson JR, et al.
**摘要**:利用冷冻电镜技术解析了重组BCL2L2蛋白与BAK的复合物结构,揭示了BCL2L2通过α-螺旋结构域结合BAK的BH3结构域,阻断BAK激活的分子机制,为设计靶向BCL2家族蛋白的抗癌药物提供了结构基础。
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3. **文献名称**:*BCL2L2 recombinant protein suppresses chemotherapy-induced apoptosis in colorectal cancer cells*
**作者**:Li H, et al.
**摘要**:研究发现,外源性添加重组BCL2L2蛋白可降低结直肠癌细胞对奥沙利铂的敏感性,其机制与抑制Caspase-3活化及PARP剪切有关。该结果提示BCL2L2过表达可能与肿瘤耐药性相关。
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**备注**:以上文献为示例性内容,实际引用时请通过PubMed或期刊数据库核实具体信息。如需扩展,可关注BCL2L2在癌症、神经退行性疾病中的双重作用研究。
**Background of BCL2L2 Recombinant Protein**
BCL2L2. commonly known as BCL-W, is a member of the BCL-2 protein family, which plays a pivotal role in regulating mitochondrial-dependent apoptosis. Encoded by the *BCL2L2* gene, this anti-apoptotic protein shares structural homology with other BCL-2 family members, including conserved BCL-2 homology (BH) domains (BH1-BH4). BCL-W primarily inhibits apoptosis by binding pro-apoptotic proteins like BAX and BAK, thereby preventing mitochondrial outer membrane permeabilization (MOMP) and blocking cytochrome *c* release, a key step in the intrinsic apoptosis pathway.
Recombinant BCL2L2 protein is engineered using expression systems such as *E. coli* or mammalian cells, ensuring proper folding and post-translational modifications for functional studies. Purification techniques like affinity chromatography yield high-purity protein, often tagged for detection (e.g., His or GST tags). This recombinant tool is widely used to study protein-protein interactions, screen small-molecule inhibitors, and elucidate structural mechanisms of apoptosis regulation.
BCL-W is implicated in cancer progression, where its overexpression in tumors (e.g., colorectal, glioblastoma) confers resistance to chemotherapy. Consequently, recombinant BCL2L2 aids in developing BH3 mimetics—drugs that disrupt anti-apoptotic interactions to restore cell death in malignancies. Beyond oncology, it contributes to research on neurodegenerative diseases and tissue homeostasis. However, its tissue-specific ___expression (e.g., in testes and neurons) suggests nuanced roles beyond general apoptosis inhibition, warranting further exploration.
Overall, BCL2L2 recombinant protein serves as a critical reagent for dissecting apoptotic pathways and advancing targeted therapies, highlighting its dual significance in basic research and translational medicine.
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