| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | ribA |
| Uniprot No | P0A7I7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-196aa |
| 氨基酸序列 | MQLKRVAEAKLPTPWGDFLMVGFEELATGHDHVALVYGDISGHTPVLARVHSECLTGDALFSLRCDCGFQLEAALTQIAEEGRGILLYHRQEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADERDFTLCADMFKLLGVNEVRLLTNNPKKVEILTEAGINIVERVPLIVGRNPNNEHYLDTKAEKMGHLLNK |
| 预测分子量 | 25.8 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ribA重组蛋白的3篇参考文献的简要信息：
1. **文献名称**：*Cloning and expression of the ribA gene encoding GTP cyclohydrolase II in Escherichia coli*
**作者**：Richter G, et al.
**摘要**：该研究报道了大肠杆菌ribA基因的克隆与重组表达，证明其编码的GTP环化水解酶II催化核黄素生物合成的第一步反应，重组蛋白具有酶活性，为体外研究提供工具。
2. **文献名称**：*Structural characterization of recombinant RibA from Bacillus subtilis*
**作者**：Kaiser J, et al.
**摘要**：通过重组表达枯草芽孢杆菌ribA蛋白并解析其晶体结构，揭示了该酶活性位点的关键氨基酸残基，阐明其底物特异性机制。
3. **文献名称**：*Optimization of ribA expression in Pichia pastoris for riboflavin production*
**作者**：Wang L, et al.
**摘要**：研究在毕赤酵母中优化表达ribA重组蛋白，通过发酵条件调整提高酶活性和稳定性，为工业核黄素生物合成提供了高效工程菌株构建策略。
(注：以上文献信息为模拟示例，实际文献需根据具体研究检索。)
**Background of ribA Recombinant Protein**
The ribA gene encodes a key enzyme involved in the biosynthesis of riboflavin (vitamin B₂), an essential cofactor in cellular redox reactions. In bacteria, ribA typically functions as GTP cyclohydrolase II, catalyzing the first committed step of the riboflavin pathway by converting GTP into 2.5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate. This metabolic pathway is absent in humans, making ribA a potential antimicrobial target.
Recombinant ribA protein is produced through genetic engineering, where the ribA gene is cloned into an expression vector and expressed in heterologous hosts like *Escherichia coli*. Purification via affinity chromatography yields functional ribA protein for structural and functional studies. Research on ribA focuses on elucidating riboflavin synthesis mechanisms, particularly in pathogenic bacteria that rely on endogenous riboflavin production for survival. Inhibitors targeting ribA could lead to novel antibiotics, as disrupting this enzyme may impair bacterial growth without affecting human cells.
Additionally, ribA recombinant protein serves as a tool for enzymatic assays, substrate specificity studies, and crystallography to resolve its 3D structure. Such insights aid in rational drug design. In some studies, ribA has been explored as a vaccine candidate, as antibodies against this protein might neutralize bacterial virulence. Overall, ribA recombinant protein is pivotal in understanding microbial metabolism and advancing therapeutic strategies against antibiotic-resistant pathogens.
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