| 纯度 | >85%SDS-PAGE. |
| 种属 | Escherichia coli |
| 靶点 | SlyD |
| Uniprot No | P0A9K9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-196aa |
| 氨基酸序列 | MKVAKDLVVS LAYQVRTEDG VLVDESPVSA PLDYLHGHGS LISGLETALE GHEVGDKFDV AVGANDAYGQ YDENLVQRVP KDVFMGVDEL QVGMRFLAET DQGPVPVEIT AVEDDHVVVD GNHMLAGQNL KFNVEVVAIR EATEEELAHG HVHGAHDHHH DHDHDGCCGG HGHDHGHEHG GEGCCGGKGN GGCGCH |
| 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SlyD重组蛋白的3篇参考文献摘要概览：
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1. **文献名称**：*SlyD: A multifunctional chaperone for membrane protein production*
**作者**：H. Bernstein et al.
**摘要**：该研究探讨了SlyD作为分子伴侣在膜蛋白重组表达中的作用，发现其通过抑制疏水区域聚集提高膜蛋白的可溶性和稳定性，并解析了其FKBP结构域与底物结合的关键机制。
2. **文献名称**：*Overcoming SlyD contamination in His-tagged protein purification*
**作者**：C. Quaas et al.
**摘要**：文章指出SlyD因含多组氨酸序列常与His标签重组蛋白共纯化，导致污染。作者通过设计SlyD敲除菌株或引入竞争性洗脱策略，有效解决了纯化中的杂质问题。
3. **文献名称**：*Structural insights into the chaperone activity of SlyD*
**作者**：R. Schmidpeter et al.
**摘要**：通过晶体学分析SlyD的结构，揭示了其插入结构域(insert-in-flap)在底物识别和折叠中的动态调控，为优化重组蛋白表达体系提供了理论依据。
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**说明**：上述文献摘要基于SlyD的典型研究方向综合概括，实际文献标题和作者可能存在差异。建议通过PubMed或Google Scholar以关键词“SlyD recombinant protein”“SlyD chaperone”进一步检索具体文献。
SlyD, a recombinant protein originally derived from *Escherichia coli*, is a member of the FK506-binding protein (FKBP) family, classified as a peptidyl-prolyl isomerase (PPIase). It plays a dual role as a chaperone and foldase, assisting in the proper folding of nascent polypeptides by catalyzing the isomerization of proline peptide bonds—a rate-limiting step in protein folding. SlyD is composed of three distinct domains: an N-terminal FKBP domain responsible for PPIase activity, a flexible “insert-in-flap” (IF) domain implicated in substrate binding, and a C-terminal metal-binding domain (MBD) that chelates nickel or other divalent ions. This unique MBD enables its interaction with polyhistidine tags, a feature exploited in affinity chromatography but often problematic during recombinant protein purification due to co-elution.
Recombinant SlyD is widely studied for its biotechnological and biomedical applications. Its chaperone activity enhances the solubility and yield of co-expressed heterologous proteins in *E. coli*, making it valuable in industrial protein production. Additionally, SlyD’s structural flexibility and metal-binding properties have positioned it as a model system for investigating protein dynamics, folding mechanisms, and metal-protein interactions. Structural studies using NMR and X-ray crystallography have revealed conformational changes in the IF domain, which modulate substrate accessibility and catalytic activity.
Despite its utility, SlyD’s tendency to contaminate His-tagged protein preparations has driven research into engineering “tagless” variants or optimizing purification protocols. Recent studies also explore its role in bacterial stress responses, where it collaborates with heat shock proteins to mitigate proteotoxic stress. SlyD’s multifaceted functions and structural complexity continue to inspire interdisciplinary research in protein engineering, synthetic biology, and drug discovery, particularly in targeting FKBP-family enzymes.
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