| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | gmhA |
| Uniprot No | P63224 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-192aa |
| 氨基酸序列 | MYQDLIRNELNEAAETLANFLKDDANIHAIQRAAVLLADSFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAIAISDVSHISCVGNDFGFNDIFSRYVEAVGREGDVLLGISTSGNSANVIKAIAAAREKGMKVITLTGKDGGKMAGTADIEIRVPHFGYADRIQEIHIKVIHILIQLIEKEMVK |
| 预测分子量 | 36.8 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. |
以下是模拟生成的关于gmhA重组蛋白的参考文献示例，供参考使用(注：非真实文献，内容为虚构)：
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1. **标题**: *Cloning and Functional Characterization of Recombinant gmhA Protein in Salmonella typhimurium*
**作者**: Smith J, Brown K, et al.
**摘要**: 本研究成功在大肠杆菌中克隆并表达了来自鼠伤寒沙门氏菌的gmhA基因，通过亲和层析纯化获得高纯度重组蛋白。酶活实验表明，该蛋白具有磷酸庚糖异构酶活性，证实其在脂多糖(LPS)合成中的关键作用。
2. **标题**: *Crystal Structure of gmhA-Encoded Enzyme Reveals Catalytic Mechanism in LPS Biosynthesis*
**作者**: Lee S, Watanabe T, et al.
**摘要**: 通过X射线晶体学解析了重组gmhA蛋白的三维结构(分辨率2.1 Å)，揭示了其底物结合位点及催化残基，为针对革兰氏阴性菌的抑制剂设计提供了结构基础。
3. **标题**: *Role of Recombinant gmhA in Bacterial Virulence: Insights from Knockout Complementation Studies*
**作者**: Zhang Y, Chen L, et al.
**摘要**: 在铜绿假单胞菌中敲除gmhA导致LPS合成缺陷和毒力显著降低，而回补重组gmhA蛋白后毒力恢复，证明其在病原菌感染中的必要性。
4. **标题**: *Optimization of gmhA Recombinant Expression for High-Throughput Antibacterial Screening*
**作者**: Johnson R, et al.
**摘要**: 开发了一种基于昆虫细胞表达系统的gmhA重组蛋白规模化生产策略，并建立了高通量酶抑制检测体系，用于筛选潜在抗菌化合物。
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如需真实文献，建议通过PubMed或Google Scholar检索关键词“gmhA recombinant protein”“phosphoheptose isomerase expression”等获取。
**Background of GmhA Recombinant Protein**
GmhA, encoded by the *gmhA* gene, is a critical enzyme in the biosynthesis of ADP-L-*glycero*-β-D-*manno*-heptose (ADP-L,D-heptose), a key component of the lipopolysaccharide (LPS) layer in Gram-negative bacteria. LPS, a major constituent of the outer membrane, plays essential roles in bacterial viability, pathogenicity, and host immune evasion. GmhA catalyzes the first committed step in the heptose biosynthesis pathway, converting D-sedoheptulose 7-phosphate to D-glycero-D-manno-heptose 7-phosphate. This reaction is pivotal for assembling the inner core oligosaccharide of LPS, which influences bacterial resistance to antimicrobial agents and interaction with host defenses.
Recombinant GmhA protein is produced through heterologous __expression (e.g., in *E. coli*) for structural and functional studies. Its purification enables detailed biochemical characterization, including substrate specificity, kinetics, and inhibition assays. Research on GmhA has gained attention due to its potential as a therapeutic target. Inhibiting GmhA disrupts LPS biosynthesis, compromising bacterial membrane integrity and enhancing susceptibility to antibiotics or immune clearance. This makes it a promising candidate for developing novel antimicrobials, particularly against multidrug-resistant pathogens like *Pseudomonas aeruginosa* and *Klebsiella pneumoniae*.
Structural studies (e.g., X-ray crystallography) of recombinant GmhA have revealed conserved active-site residues and mechanistic insights, guiding rational drug design. Additionally, GmhA’s role in LPS-mediated inflammation has spurred interest in understanding host-pathogen interactions and sepsis mechanisms. Despite its bacterial origin, GmhA’s conservation across Gram-negative species underscores its broad relevance in microbiology and infectious disease research.
In summary, GmhA recombinant protein serves as a vital tool for exploring bacterial pathogenesis, antibiotic development, and LPS-related immunology, addressing pressing challenges in combating resistant infections.
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