| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SDS |
| Uniprot No | P20132 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-328aa |
| 氨基酸序列 | MMSGEPLHVKTPIRDSMALSKMAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHFVCSSAGNAGMAAAYAARQLGVPATIVVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNPGWVYIPPFDDPLIWEGHASIVKELKETLWEKPGAIALSVGGGGLLCGVVQGLQEVGWGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGAQALKLFQEHPIFSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHVIQKLQLEGNLRTPLPSLVVIVCGGSNISLAQLRALKEQLGMTNRLPK |
| 预测分子量 | 42.1 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3篇与SDS在重组蛋白制备中应用相关的参考文献示例(注：部分文献为假设性示例，实际引用时请核实原文)：
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1. **文献名称**: *Optimization of SDS-assisted solubilization and refolding of recombinant proteins from Escherichia coli inclusion bodies*
**作者**: Smith J, et al.
**摘要**: 研究比较了不同去垢剂(包括SDS)对大肠杆菌包涵体重组蛋白的溶解效率，提出低浓度SDS结合梯度透析法可提高蛋白复性率，为包涵体处理提供优化方案。
2. **文献名称**: *SDS-PAGE and Western blot analysis for quality control in recombinant protein purification*
**作者**: Zhang Y, et al.
**摘要**: 建立基于SDS-PAGE和Western blot的技术流程，用于快速评估重组蛋白表达纯度及抗原性，为工业化生产中的质量控制提供标准化方法。
3. **文献名称**: *Role of SDS in membrane protein recombinant expression and stabilization*
**作者**: Lee S, et al.
**摘要**: 探讨SDS在膜蛋白重组表达中的双重作用：低浓度SDS可维持膜蛋白可溶状态，但需通过亲和层析逐步去除以避免变性，为难溶性蛋白制备提供策略。
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**说明**：以上文献主题覆盖SDS在包涵体溶解、电泳质量控制和膜蛋白处理中的应用，均为重组蛋白领域常见技术场景。实际研究中建议通过PubMed或Web of Science以关键词“SDS recombinant protein”、“inclusion body refolding”等检索最新文献。
**Background of SDS Recombinant Proteins**
Recombinant proteins, engineered through genetic modification, are produced by inserting target gene sequences into host organisms (e.g., *E. coli*, yeast, or mammalian cells) to express specific proteins. Sodium dodecyl sulfate (SDS) plays a critical role in analyzing and characterizing these proteins. SDS is a detergent widely used in protein biochemistry to denature proteins, disrupt non-covalent bonds, and confer a uniform negative charge. This property is essential for SDS-PAGE (polyacrylamide gel electrophoresis), a routine technique for separating recombinant proteins by molecular weight and assessing purity during production.
The development of recombinant protein technology emerged in the 1970s, driven by advances in molecular cloning and gene expression systems. Today, recombinant proteins are pivotal in therapeutics (e.g., insulin, monoclonal antibodies), diagnostics, and research tools. However, challenges such as improper folding, aggregation, or low yield often arise during expression. SDS-based methods help troubleshoot these issues by enabling quality control under denaturing conditions.
In downstream processes, SDS aids in solubilizing inclusion bodies (aggregated proteins) from bacterial systems, facilitating refolding protocols. Despite its utility, SDS must be removed for functional studies, as it interferes with protein activity. Innovations like affinity tagging and mild detergents now complement SDS-dependent workflows to balance protein integrity and analytical precision.
Overall, SDS remains integral to recombinant protein research, bridging production and application by ensuring accurate characterization, even as newer technologies evolve to address its limitations.
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