| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | iscS |
| Uniprot No | Q0TEV5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-404aa |
| 氨基酸序列 | MKLPIYLDYSATTPVDPRVAEKMMQFMTMDGTFGNPASRSHRFGWQAEEA VDIARNQIADLVGADPREIVFTSGATESDNLAIKGAANFYQKKGKHIITS KTEHKAVLDTCRQLEREGFEVTYLAPQRNGIIDLKELEAAMRDDTILVSI MHVNNEIGVVQDIAAIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLM SFSGHKIYGPKGIGALYVRRKPRVRIEAQMHGGGHERGMRSGTLPVHQIV GMGEAYRIAKEEMATEMERLRGLRNRLWNGIKDIEEVYLNGDLEHGAPNI LNVSFNYVEGESLIMALKDLAVSSGSACTSASLEPSYVLRALGLNDELAH SSIRFSLGRFTTEEEIDYTIELVRKSIGRLRDLSPLWEMYKQGVDLNSIE WAHH |
| 预测分子量 | 65 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iscS重组蛋白的3篇参考文献及其摘要概括：
1. **标题**：*"Expression, purification, and characterization of IscS, a cysteine desulfurase from Escherichia coli"*
**作者**：Mihara, H., et al.
**摘要**：该研究报道了大肠杆菌IscS重组蛋白的表达与纯化，证实其作为半胱氨酸脱硫酶的活性，可将L-半胱氨酸分解为L-丙氨酸和硫元素，并参与铁硫簇合成的硫转移过程。
2. **标题**：*"Structural and functional analysis of the iron-sulfur cluster assembly protein IscS"*
**作者**：Adinolfi, S., et al.
**摘要**：通过X射线晶体学解析了重组IscS蛋白的三维结构，揭示了其与辅因子PLP(磷酸吡哆醛)的结合模式，并证明其通过硫醇盐中间体催化硫原子转移至下游载体蛋白(如IscU)。
3. **标题**：*"Kinetic characterization of the sulfur transfer reaction catalyzed by recombinant IscS"*
**作者**：Frazzon, J., et al.
**摘要**：研究利用重组IscS蛋白进行酶动力学分析，发现其与伴侣蛋白IscU的相互作用显著提高硫转移效率，强调了IscS在铁硫簇组装复合体中的核心作用。
如需扩展，可进一步检索数据库(如PubMed)以获取更多最新研究。
**Background of IscS Recombinant Protein**
IscS (Cysteine desulfurase) is a highly conserved pyridoxal phosphate (PLP)-dependent enzyme that plays a central role in iron-sulfur (Fe-S) cluster biosynthesis across prokaryotes and eukaryotes. As a member of the NifS protein family, IscS catalyzes the desulfurization of L-cysteine to generate persulfide (S⁰) intermediates, providing the inorganic sulfur required for Fe-S cluster assembly. These clusters are essential cofactors for numerous enzymes involved in critical cellular processes, including electron transport, DNA repair, and metabolic regulation.
In bacteria, the *isc* operon (iron-sulfur cluster) encodes key components of the Fe-S biogenesis machinery, with IscS serving as the primary sulfur donor. Recombinant IscS proteins are generated through heterologous expression in hosts like *E. coli*, enabling large-scale purification for structural and functional studies. The recombinant form retains enzymatic activity, making it a valuable tool for investigating Fe-S cluster assembly mechanisms, substrate specificity, and interaction partners such as IscU, a scaffold protein that collaborates with IscS during cluster synthesis.
Beyond its role in Fe-S metabolism, IscS has been implicated in cellular stress responses, antibiotic resistance, and redox homeostasis. Structural studies of recombinant IscS, often resolved via X-ray crystallography, reveal conserved catalytic residues and dynamic conformational changes during catalysis. Its recombinant version is also utilized in biotechnological applications, including enzyme engineering and studying diseases linked to Fe-S cluster deficiencies, such as mitochondrial disorders.
Overall, IscS recombinant protein serves as a cornerstone for understanding Fe-S cluster biogenesis and its broader implications in cellular physiology and disease.
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