| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | ghrA |
| Uniprot No | B7LFE3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-312aa |
| 氨基酸序列 | MDIIFYHPTFDTQWWIEALRKAIPQARVRAWKSGDNDSADYALVWHPPVEMLAGRDLKAVFALGAGVDSILSKLQAHPEMLNPSVPLFRLEDTGMGEQMQEYAVSQVLHWFRRFDDYRIQQNSSHWQPLPEYHREDFTIGILGAGVLGSKVAQSLQTWRFPLRCWSRTRKSWPGVQSFAGREELSAFLSQCRVLINLLPNTPETVGIINQQLLEKLPDGAYLLNLARGVHVVEDDLLAALDSGKVKGAMLDVFNREPLPPENPLWQHPRVTITPHVAAITRPAEAVEYISRTIAQLEKGERVCGQVDRARGY |
| 预测分子量 | 51.4 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 **ghrA重组蛋白** 的示例参考文献(内容为模拟，仅供参考)：
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1. **《Cloning and Functional Characterization of Recombinant ghrA Protein in Bacillus subtilis》**
*作者：Wang et al.*
**摘要**：研究通过在大肠杆菌中克隆并表达枯草芽孢杆菌来源的ghrA基因，纯化获得重组蛋白，验证其作为谷氨酰胺合成酶的功能，并探讨其在氮代谢中的作用。
2. **《Structural Insights into ghrA Recombinant Protein by X-ray Crystallography》**
*作者：Johnson & Müller*
**摘要**：利用X射线晶体学解析ghrA重组蛋白的三维结构，揭示其活性位点特征，为酶催化机制和抑制剂设计提供依据。
3. **《ghrA Recombinant Protein Enhances Stress Tolerance in Transgenic Plants》**
*作者：Chen et al.*
**摘要**：将ghrA重组蛋白导入拟南芥中，证明其通过调节脯氨酸合成途径显著提高植物对干旱和盐胁迫的抗性。
4. **《Optimized Production of ghrA Recombinant Protein for Industrial Applications》**
*作者：Rodriguez et al.*
**摘要**：开发了一种高效表达ghrA重组蛋白的发酵工艺，评估其在生物肥料生产中的潜力，并优化酶活性和稳定性。
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**注意**：以上文献为示例，实际研究需通过 **PubMed、Google Scholar** 或 **Web of Science** 等平台，以关键词“ghrA recombinant protein”检索最新成果。
**Background of ghrA Recombinant Protein**
The *ghrA* gene, originally identified in certain bacterial species, encodes a protein implicated in stress response and cellular homeostasis. Homologs of *ghrA* are conserved across diverse organisms, suggesting its fundamental role in metabolic regulation. In bacteria like *Bacillus subtilis*, GhrA is associated with glutathione metabolism, functioning as a glutathione reductase or a redox-sensitive enzyme critical for maintaining cellular redox balance. This protein helps mitigate oxidative stress by regenerating reduced glutathione, a key antioxidant, thereby protecting cells from reactive oxygen species (ROS) damage during environmental challenges.
Recombinant GhrA protein is engineered through molecular cloning, where the *ghrA* gene is inserted into expression vectors (e.g., *E. coli* plasmids) for large-scale production. Purification techniques like affinity chromatography yield high-purity protein, enabling functional and structural studies. Researchers utilize recombinant GhrA to explore its enzymatic mechanisms, substrate specificity, and interactions with other redox-related proteins.
Beyond basic research, GhrA has biotechnological applications. Its redox-regulating properties are leveraged in industrial processes requiring oxidative stress resistance, such as biofuel production or bioremediation. In medicine, understanding GhrA's role in bacterial stress adaptation could inform strategies to combat antibiotic-resistant pathogens. Additionally, plant studies suggest analogous proteins might enhance crop resilience under abiotic stress.
Despite progress, questions remain about GhrA's regulatory networks and species-specific functional variations. Ongoing research aims to unravel its structural dynamics and potential as a therapeutic or agricultural tool, highlighting its significance in both microbial physiology and applied sciences.
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