| 纯度 | >95 % HPLC. |
| 种属 | Human |
| 靶点 | Bcl2 |
| Uniprot No | P10415 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-211aa |
| 氨基酸序列 | MAHAGRTGYDNREIVMKYIHYKLSQRGYEWDAGDVGAAPPGAAPAPGIFS SQPGHTPHPAASRDPVARTSPLQTPAAPGAAAGPALSPVPPVVHLTLRQA GDDFSRRYRRDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIVAF FEFGGVMCVESVNREMSPLVDNIALWMTEYLNRHLHTWIQDNGGWDAFVE LYGPSMRPLFD |
| 预测分子量 | 26 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Bcl-2重组蛋白的关键文献概览：
1. **"Structure of Bcl-xL-Bak peptide complex"**
*作者：Sattler M, et al. (1997. Science)*
摘要：通过X射线晶体学解析了重组Bcl-xL蛋白与促凋亡Bak肽段的复合物结构，揭示了BH3结构域如何通过疏水相互作用调控凋亡的分子机制。
2. **"Bcl-2 gene promotes haemopoietic cell survival"**
*作者：Vaux DL, et al. (1988. Nature)*
摘要：首次证实重组Bcl-2蛋白通过抑制程序性死亡延长细胞生存，为理解凋亡调控网络奠定基础(注：经典文献建议核对最新版本)。
3. **"ABT-737 binds to Bcl-2 and Bcl-xL"**
*作者：Oltersdorf T, et al. (2005. Nature)*
摘要：利用重组Bcl-2家族蛋白筛选出小分子抑制剂ABT-737.阐明其通过占据BH3结合口袋拮抗抗凋亡功能的药物开发路径。
*注：文献选取兼顾机制解析与药物开发方向，建议通过PubMed/Web of Science核对最新研究进展。如需特定研究方向(如蛋白纯化方法)，可补充说明。*
Bcl-2 (B-cell lymphoma 2) is a critical regulatory protein involved in apoptosis, a process essential for maintaining cellular homeostasis. Discovered in 1985 through its association with chromosomal translocations in B-cell lymphomas, Bcl-2 became the founding member of a protein family characterized by conserved Bcl-2 homology (BH) domains. Unlike most oncoproteins that promote cell proliferation, Bcl-2 exerts its oncogenic effects by inhibiting programmed cell death, enabling cancer cell survival. This anti-apoptotic function is mediated through interactions with pro-apoptotic family members (e.g., Bax, Bak) via BH domains, regulating mitochondrial outer membrane permeabilization and cytochrome c release.
Recombinant Bcl-2 proteins are engineered using genetic cloning techniques to study structure-function relationships or develop therapeutic strategies. Typically produced in bacterial (e.g., E. coli) or eukaryotic expression systems, these proteins retain key domains required for apoptosis regulation. Purification often involves affinity chromatography tags (e.g., His-tag) followed by refolding steps to ensure proper conformation. Researchers utilize recombinant Bcl-2 to investigate its 3D structure, binding interfaces, and interactions with inhibitors like ABT-199 (Venetoclax), a BH3-mimetic drug approved for leukemia treatment. Additionally, these proteins serve as tools for screening small-molecule compounds targeting Bcl-2's hydrophobic groove, a hotspot for cancer therapy development. Challenges in working with recombinant Bcl-2 include maintaining solubility due to its hydrophobic regions and ensuring post-translational modifications (e.g., phosphorylation) in eukaryotic expression systems. Current studies also explore its role beyond apoptosis, including autophagy and mitochondrial dynamics. As dysregulated Bcl-2 expression is implicated in various cancers and neurodegenerative diseases, recombinant versions remain vital for both basic research and drug discovery pipelines.
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