| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | BMF |
| Uniprot No | Q96LC9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-184aa |
| 氨基酸序列 | MEPSQCVEELEDDVFQPEDGEPVTQPGSLLSADLFAQSLLDCPLSRLQLFPLTHCCGPGLRPTSQEDKATQTLSPASPSPGVMLPCGVTEEPQRLFYGNAGYRLPLPASFPAVLPIGEQPPEGQWQHQAEVQIARKLQCIADQFHRLHVQQHQQNQNRVWWQILLFLHNLALNGEENRNGAGPR |
| 预测分子量 | 47.5 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BMF重组蛋白的3篇虚构参考文献示例(仅供参考，非真实文献)：
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**1. 文献名称**：重组BMF蛋白的制备及其促凋亡活性研究
**作者**：Zhang L, Wang Y, Chen H
**摘要**：本研究通过原核表达系统成功制备了高纯度重组BMF蛋白，并验证其与抗凋亡蛋白Bcl-2的结合能力。体外实验表明，重组BMF可显著诱导HeLa细胞凋亡，提示其在癌症治疗中的潜在应用价值。
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**2. 文献名称**：BMF重组蛋白的结构解析与功能调控机制
**作者**：Smith J, Brown K, Lee S
**摘要**：利用X射线晶体学首次解析了重组BMF蛋白的三维结构，揭示了其BH3结构域的关键结合位点。通过分子动力学模拟，阐明了BMF在凋亡信号通路中与Mcl-1蛋白的相互作用机制。
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**3. 文献名称**：靶向递送BMF重组蛋白增强化疗敏感性的实验研究
**作者**：Gupta R, Patel M, Liu X
**摘要**：开发了一种基于纳米颗粒的BMF重组蛋白递送系统，可有效穿透肿瘤微环境。动物实验表明，联合化疗药物使用显著抑制了肺癌模型中的肿瘤生长，为克服耐药性提供了新策略。
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**注**：以上内容为模拟生成，实际文献需通过学术数据库(如PubMed、Web of Science)检索关键词“BMF recombinant protein”或“Bcl-2 modifying factor apoptosis”获取。
**Background of BMF Recombinant Protein**
BMF (Bcl-2-modifying factor) is a pro-apoptotic protein belonging to the Bcl-2 family, which plays a central role in regulating mitochondrial apoptosis. Discovered in the early 2000s, BMF is classified as a BH3-only protein due to its conserved Bcl-2 homology 3 (BH3) domain, critical for initiating apoptosis by neutralizing anti-apoptotic Bcl-2 family members like Bcl-2 and Bcl-xL. Under normal physiological conditions, BMF is sequestered in the cytoskeleton via interactions with myosin V and dynein light chain complexes. Cellular stress signals, such as DNA damage, cytoskeletal disruption, or growth factor deprivation, trigger BMF release, enabling it to translocate to mitochondria and promote cytochrome c release, caspase activation, and programmed cell death.
Recombinant BMF protein is engineered using molecular cloning techniques, often expressed in *E. coli* or mammalian systems to ensure proper folding and post-translational modifications. Its production enables detailed mechanistic studies of apoptosis pathways, drug discovery, and therapeutic applications. For instance, recombinant BMF serves as a tool to investigate interactions with anti-apoptotic proteins or to screen small molecules aiming to restore apoptosis in cancer cells resistant to conventional treatments.
In disease contexts, dysregulated BMF expression is linked to cancer, autoimmune disorders, and neurodegenerative conditions. Overexpression of recombinant BMF has shown potential in sensitizing tumor cells to chemotherapy, highlighting its therapeutic relevance. However, challenges remain in optimizing delivery systems and minimizing off-target effects. Current research focuses on harnessing BMF’s apoptotic activity through BH3 mimetics or gene therapy, offering promising avenues for precision medicine. Overall, BMF recombinant protein represents a vital resource for advancing both basic apoptosis research and novel therapeutic strategies.
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