| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | BAD |
| Uniprot No | Q92934 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-168aa |
| 氨基酸序列 | MFQIPEFEPS EQEDSSSAER GLGPSPAGDG PSGSGKHHRQ APGLLWDASH QQEQPTSSSH HGGAGAVEIR SRHSSYPAGT EDDEGMGEEP SPFRGRSRSA PPNLWAAQRY GRELRRMSDE FVDSFKKGLP RPKSAGTATQ MRQSSSWTRV FQSWWDRNLG RGSSAPSQ |
| 预测分子量 | 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BAD重组蛋白的3篇参考文献示例，包含文献名称、作者及摘要概括：
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1. **文献名称**: "Recombinant Production and Functional Analysis of BAD Protein in Apoptosis Regulation"
**作者**: Smith, J.D., et al.
**摘要**: 该研究报道了在大肠杆菌中成功表达并纯化带有His标签的重组BAD蛋白。通过体外结合实验证实了重组BAD与抗凋亡蛋白Bcl-xL的相互作用，并发现其促凋亡活性依赖于去磷酸化状态。
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2. **文献名称**: "Phosphorylation Mimetics of BAD Recombinant Protein Alter Mitochondrial Apoptotic Pathways"
**作者**: Chen, L., & Wang, H.
**摘要**: 作者通过定点突变技术构建了BAD的磷酸化模拟突变体(如S112D/S136D)，利用重组蛋白证明磷酸化修饰抑制了BAD与Bcl-2的结合能力，从而降低其促凋亡功能，揭示了BAD在细胞存活中的调控机制。
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3. **文献名称**: "Structural Characterization of Recombinant BAD Protein Using NMR Spectroscopy"
**作者**: Kumar, R., et al.
**摘要**: 本研究通过核磁共振(NMR)解析了重组BAD蛋白的结构，发现其N端无序区域对结合Bcl-xL至关重要。结构数据为设计靶向BAD-Bcl-2相互作用的小分子抑制剂提供了理论基础。
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*注：上述文献为示例，实际引用时需根据具体研究内容检索真实发表的论文。建议使用PubMed或Web of Science等平台以关键词“BAD recombinant protein apoptosis”进一步筛选文献。*
BAD (Bcl-2-associated death promoter) is a pro-apoptotic protein belonging to the Bcl-2 family, which regulates mitochondrial-dependent apoptosis. Discovered in the mid-1990s, BAD functions as a critical mediator of cell death by interacting with anti-apoptotic Bcl-2 family members (e.g., Bcl-2 and Bcl-xL) through its BH3 domain. This interaction neutralizes their pro-survival effects, promoting cytochrome c release from mitochondria and subsequent caspase activation. BAD’s activity is tightly regulated by phosphorylation. Survival signals, such as growth factors, activate kinases like AKT and PKA, which phosphorylate BAD at specific serine residues (e.g., Ser-112. Ser-136. and Ser-155). Phosphorylated BAD is sequestered in the cytoplasm by 14-3-3 proteins, preventing its pro-apoptotic function. Dysregulation of BAD is implicated in cancer, neurodegenerative diseases, and metabolic disorders, making it a therapeutic target.
Recombinant BAD proteins are engineered using bacterial (e.g., E. coli) or mammalian expression systems for functional studies. These proteins retain key structural features, including the BH3 domain and phosphorylation sites, enabling research on apoptosis mechanisms, protein interactions, and drug screening. Tagged versions (e.g., His-tag, GST-tag) facilitate purification and detection. Studies using recombinant BAD have elucidated its role in cell fate decisions, synergy with other BH3-only proteins, and crosstalk with metabolic pathways. Additionally, phospho-mimetic mutants (e.g., Ser→Asp/Glu substitutions) help dissect phosphorylation-dependent regulatory mechanisms. As a tool, recombinant BAD contributes to developing BH3 mimetics and personalized therapies targeting apoptotic pathways.
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