Recombinant Human SecB protein

中文名： 蛋白质输出蛋白SecB(SecB)重组蛋白
别名： secB;Protein-export protein SecB

货号: PA1000-2867

Price： ￥询价

20μg 50μg 100μg ＞100μg

数量：

大包装询价

产品详情

纯度	>90%SDS-PAGE.
种属	Human
靶点	SecB
Uniprot No	P44853
内毒素	< 0.01EU/μg
表达宿主	E.coli
表达区间	1-169aa
氨基酸序列	MSEQKQDVAATEEQQPVLQIQRIYVKDVSFEAPNLPHIFQQEWKPKLGFDLSTETTQVGDDLYEVVLNISVETTLEDSGDVAFICEVKQAGVFTISGLEDVQMAHCLTSQCPNMLFPYARELVSNLVNRGTFPALNLSPVNFDALFVEYMNRQQAENAEEKSEEEQTKH
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.

参考文献

以下是关于SecB重组蛋白的3篇参考文献概览：

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1. **文献名称**: *"SecB Chaperone in Protein Export: Mechanism of Substrate Recognition"*

**作者**: Kumamoto, C. A. 等

**摘要**: 该研究探讨SecB分子伴侣如何识别未折叠的底物蛋白并协助其跨膜转运的机制，发现SecB通过结合底物的疏水区域防止聚集，从而提升重组蛋白在大肠杆菌中的稳定性与分泌效率。

2. **文献名称**: *"Enhancing Solubility of Recombinant Proteins by Co-expression with SecB in E. coli"*

**作者**: Ullers, R. S. 等

**摘要**: 文章提出通过共表达SecB与目标重组蛋白，显著提高难溶蛋白的可溶性产量。实验表明，SecB延缓了蛋白折叠速度，减少包涵体形成，适用于工业规模的重组蛋白生产优化。

3. **文献名称**: *"Functional Analysis of SecB Mutants in Recombinant Protein Secretion"*

**作者**: Nicolaus, F. 等

**摘要**: 研究通过构建SecB突变体，揭示其C端结构域对底物结合的关键作用。实验证明特定突变体可增强重组蛋白的跨膜转运能力，为工程化改造分子伴侣以优化蛋白分泌系统提供理论支持。

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以上文献均聚焦于SecB在重组蛋白表达、折叠及分泌中的作用机制与应用潜力，涵盖基础机制与生物技术应用场景。如需具体文章，可进一步通过PubMed或Sci-Hub获取全文。

背景信息

**Background of SecB Chaperone in Recombinant Protein Production**

SecB is a cytosolic molecular chaperone primarily found in *Escherichia coli* and other Gram-negative bacteria. It plays a critical role in maintaining newly synthesized polypeptides in an unfolded, translocation-competent state, ensuring their efficient secretion via the Sec (secretory) pathway. This ATP-independent chaperone binds to nascent or stress-denatured proteins, preventing premature folding or aggregation, particularly under conditions of high metabolic activity or environmental stress.

In recombinant protein production, SecB is notable for its ability to enhance the solubility and yield of heterologous proteins expressed in bacterial systems. When co-expressed with target proteins, it stabilizes unstable folding intermediates, reducing inclusion body formation—a common challenge in *E. coli*-based expression. Its substrate-binding mechanism involves recognizing exposed hydrophobic regions on unfolded polypeptides, a feature exploited in biotechnology to improve the folding of complex or aggregation-prone proteins.

Structurally, SecB functions as a tetramer, forming dynamic complexes with client proteins. Unlike ATP-dependent chaperones (e.g., GroEL/ES), SecB does not actively fold proteins but acts as a "holdase," delivering substrates to the Sec translocon for membrane transport or to other folding machinery. This transient interaction makes it particularly useful in processes requiring rapid protein export, such as recombinant secretion systems.

Research on SecB has advanced bioprocessing strategies, particularly for industrial enzymes, therapeutic proteins, and antigens. Its application in co-expression systems underscores its importance in optimizing soluble protein production, addressing bottlenecks in both academic research and large-scale biomanufacturing.