| 纯度 | >85%SDS-PAGE. |
| 种属 | Dickeya dadantii |
| 靶点 | DsbC |
| Uniprot No | P39691 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-238aa |
| 氨基酸序列 | DDAAIKQTL NRLGLQSAEV KDSPIGGMKT VLTENGVLYI TEDGKHLLQG PLYDVSGKTP VNVTNHILNE RLDALKDQMI VYKAPQEKHV ITVFTDITCG YCHKLHEQMK DYNALGITVR YLAYPRQGMN SQAAKDMQSI WCVADRNKAF DAAMKGDDVS PATCKTDIGA HYQLGVLFGV QGTPAIVLDD GTVVPGYQPP KEMMAMLDAH KASLKSGG |
| 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DsbC重组蛋白的3篇参考文献示例，涵盖结构、功能及应用研究：
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1. **文献名称**：*Crystal structure of the DsbC protein (PDB ID: 1EEJ) reveals a functional dimeric enzyme with a thioredoxin fold*
**作者**：McCarthy, A.A., Haebel, P.W., Torronen, A., et al.
**摘要**：该研究解析了DsbC的晶体结构，揭示其作为二聚体蛋白的硫氧还蛋白折叠特征，并阐明了其底物结合口袋的结构基础，解释了其作为二硫键异构酶的催化机制。
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2. **文献名称**：*DsbC enhances solubility and facilitates correct disulfide bond formation in recombinant proteins expressed in E. coli*
**作者**：Bessette, P.H., Aslund, F., Beckwith, J., & Bardwell, J.C.A.
**摘要**：本文证明在大肠杆菌中过表达DsbC可显著提高含复杂二硫键的重组蛋白(如抗体片段)的溶解度和正确折叠率，为优化重组蛋白生产提供策略。
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3. **文献名称**：*Redox properties and functional interplay of DsbC with DsbD in the bacterial periplasm*
**作者**：Rietsch, A., Bessette, P., Georgiou, G., & Beckwith, J.
**摘要**：研究探讨了DsbC与还原酶DsbD的氧化还原互作机制，发现DsbD通过维持DsbC的还原状态，确保其持续催化错误二硫键的异构化功能，深化了对细菌周质氧化还原网络的认知。
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以上文献涵盖结构解析、重组应用及分子机制，均为DsbC研究领域的代表性工作。如需更具体的文献，建议通过PubMed或Google Scholar检索近年研究。
DsbC is a periplasmic disulfide bond isomerase in Gram-negative bacteria, primarily studied in *Escherichia coli*. It belongs to the Dsb protein family, which regulates oxidative folding of secreted proteins. Unlike its oxidase counterpart DsbA, which catalyzes disulfide bond formation, DsbC specializes in rearranging incorrect disulfide linkages—a critical function for proteins with complex tertiary structures. This isomerase activity makes DsbC particularly valuable in recombinant protein production, where misfolded disulfide bonds are common challenges.
Structurally, DsbC forms a homodimer linked by a central helical domain, creating a V-shaped scaffold. Each monomer contains a thioredoxin-like domain with a CXXC catalytic motif. Its isomerase activity relies on maintaining a reduced state, regulated by the inner membrane protein DsbD. This redox control allows DsbC to act as both a chaperone and a proofreader, resolving kinetically trapped folding intermediates.
In biotechnology, recombinant DsbC is widely co-expressed to enhance yields of properly folded eukaryotic proteins in bacterial systems. Its ability to correct disulfide mismatches improves the solubility and functionality of recombinant products, especially antibodies, cytokines, and enzymes. Researchers also utilize purified DsbC in *in vitro* refolding protocols. Beyond industrial applications, studies on DsbC have advanced fundamental understanding of oxidative protein folding, inspiring engineering of artificial chaperones. However, its dimeric nature and redox sensitivity pose challenges for heterologous expression, driving optimization of production strains and purification strategies.
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