| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | grxD |
| Uniprot No | P0AC69 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-115aa |
| 氨基酸序列 | MSTTIEKIQR QIAENPILLY MKGSPKLPSC GFSAQAVQAL AACGERFAYV DILQNPDIRA ELPKYANWPT FPQLWVDGEL VGGCDIVIEM YQRGELQQLI KETAAKYKSE EPDAE |
| 预测分子量 | 12,8 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GrxD重组蛋白的3篇参考文献示例(注：文献为虚拟示例，仅供参考格式)：
1. **标题**：*Heterologous Expression and Functional Analysis of GrxD in Bacillus subtilis*
**作者**：Chen L, Wang Y
**摘要**：该研究在大肠杆菌中克隆并表达了来自枯草芽孢杆菌的GrxD基因，证实重组蛋白具有硫氧还蛋白活性，可增强宿主菌对过氧化氢胁迫的抗性。
2. **标题**：*Crystal Structure of Recombinant GrxD Reveals a Unique Disulfide Bond Mechanism*
**作者**：Kim S, et al.
**摘要**：通过X射线晶体学解析了重组GrxD的三维结构，发现其活性位点的二硫键动态变化机制，为理解其氧化还原调控功能提供结构基础。
3. **标题**：*GrxD Recombinant Protein Enhances Iron-Sulfur Cluster Assembly in Vitro*
**作者**：Müller F, et al.
**摘要**：研究证明重组GrxD蛋白在体外实验中可促进铁硫簇的组装，并依赖谷胱甘肽作为辅因子，提示其在细胞代谢中的关键作用。
*注：若需真实文献，建议在PubMed或Google Scholar中以“GrxD recombinant protein”或“Glutaredoxin D expression”为关键词检索。*
**Background of GrxD Recombinant Protein**
GrxD recombinant protein is a engineered form of glutathione reductase-like protein D (GrxD), a member of the thioredoxin superfamily, which plays a critical role in maintaining cellular redox homeostasis. GrxD proteins are redox enzymes involved in electron transfer reactions, primarily facilitating the reduction of disulfide bonds in substrate proteins via a conserved cysteine-containing active site (CXXC motif). These proteins are essential in protecting cells against oxidative stress by scavenging reactive oxygen species (ROS) and repairing oxidative damage to critical biomolecules.
In bacteria, such as *Escherichia coli*, GrxD homologs are part of the glutaredoxin system, working synergistically with glutathione (GSH) and NADPH-dependent glutathione reductase to regulate thiol-disulfide balance. GrxD specifically participates in iron-sulfur (Fe-S) cluster biosynthesis and transfer, a process vital for the function of numerous metalloproteins involved in DNA repair, energy metabolism, and signal transduction.
Recombinant GrxD is produced using genetic engineering techniques, where the *grxD* gene is cloned into expression vectors and overexpressed in host systems (e.g., *E. coli* or yeast). The protein is then purified via affinity chromatography, often incorporating tags like His-tags for ease of isolation. Its recombinant form retains native enzymatic activity, making it a valuable tool for *in vitro* studies, including mechanistic investigations of Fe-S cluster assembly, redox signaling pathways, and antioxidant defense mechanisms.
Research on GrxD recombinant protein has implications for understanding microbial stress adaptation, industrial biotechnology (e.g., optimizing oxidative stress-resistant strains), and human health, as dysregulation of redox systems is linked to diseases like cancer and neurodegeneration. Its study also aids in developing novel antimicrobial agents targeting bacterial redox homeostasis.
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