| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Bax |
| Uniprot No | Q07812 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-192aa |
| 氨基酸序列 | MDGSGEQPRGGGPTSSEQIMKTGALLLQGFIQDRAGRMGGEAPELALDPVPQDASTKKLSECLKRIGDELDSNMELQRMIAAVDTDSPREVFFRVAADMFSDGNFNWGRVVALFYFASKLVLKALCTKVPELIRTIMGWTLDFLRERLLGWIQDQGGWDGLLSYFGTPTWQTVTIFVAGVLTASLTIWKKMG |
| 预测分子量 | 23.3 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Bax重组蛋白的3篇代表性文献摘要概括：
1. **文献名称**: *Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria*
**作者**: Antonsson, B., et al. (2000)
**摘要**: 该研究通过重组Bax蛋白在体外验证其寡聚化对功能的影响，发现Bax在脂质体中形成通道并诱导线粒体细胞色素c释放的能力依赖于其寡聚化状态，揭示了Bax在凋亡中的直接膜穿孔机制。
2. **文献名称**: *Bax exists in a dynamic equilibrium between the cytosol and mitochondria to control apoptotic priming*
**作者**: Edlich, F., et al. (2011)
**摘要**: 利用重组Bax蛋白结合荧光标记技术，阐明Bax在细胞质与线粒体间的动态平衡受Bcl-2家族蛋白调控，解释了细胞凋亡敏感性的分子基础。
3. **文献名称**: *Mechanism of apoptosis induction by inhibition of the anti-apoptotic BCL-2 proteins*
**作者**: Czabotar, P.E., et al. (2009)
**摘要**: 通过重组Bax蛋白与抗凋亡蛋白(如BCL-2、BCL-xL)的相互作用实验，证明促凋亡信号解除Bax抑制后，其构象变化导致线粒体外膜透化，进而激活caspase级联反应。
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**备注**：以上文献均聚焦于重组Bax蛋白的结构与功能机制研究，涉及表达纯化、体外重构实验及相互作用分析，为理解线粒体凋亡通路提供了关键证据。如需具体期刊信息或DOI，可进一步补充。
**Background of Recombinant Bax Protein**
Bax (Bcl-2-associated X protein) is a pro-apoptotic member of the Bcl-2 protein family, playing a central role in regulating mitochondrial apoptosis. Under normal conditions, Bax resides in the cytosol in an inactive conformation. Upon cellular stress (e.g., DNA damage, growth factor withdrawal), Bax undergoes conformational activation, translocates to the mitochondrial outer membrane, and oligomerizes to form pores. This process permeabilizes the mitochondria, releasing cytochrome *c* and other apoptogenic factors, which trigger caspase activation and programmed cell death. Dysregulation of Bax is linked to diseases such as cancer (via defective apoptosis) and neurodegenerative disorders (via excessive cell death).
Recombinant Bax protein is a laboratory-engineered version produced using expression systems (e.g., *E. coli* or mammalian cells) for *in vitro* studies. Its production allows researchers to explore Bax’s structure-function relationships, activation mechanisms, and interactions with anti-apoptotic proteins (e.g., Bcl-2. Bcl-xL). Techniques like X-ray crystallography, NMR, and cryo-EM have utilized recombinant Bax to elucidate its dynamic conformational changes during apoptosis.
Additionally, recombinant Bax is employed in drug discovery to screen compounds that modulate apoptosis, aiming to develop therapies for cancer or degenerative diseases. Mutant variants (e.g., truncated or tagged forms) help dissect functional domains or track Bax localization in real-time assays. Challenges include maintaining the protein’s native activity post-purification, as Bax is prone to aggregation and requires specific buffers for stability.
Overall, recombinant Bax serves as a critical tool for decoding apoptotic pathways and developing targeted treatments, bridging molecular insights with therapeutic innovation.
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