| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | thiO |
| Uniprot No | P09110 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 27-331aa |
| 氨基酸序列 | LSGAPQASAADVVVVHGRRTAICRAGRGGFKDTTPDELLSAVMTAVLKDVNLRPEQLGDICVGNVLQPGAGAIMARIAQFLSDIPETVPLSTVNRQCSSGLQAVASIAGGIRNGSYDIGMACGITSENVAERFGISREKQDTFALASQQKAARAQSKGCFQAEIVPVTTTVHDDKGTKRSITVTQDEGIRPSTTMEGLAKLKPAFKKDGSTTAGLTVSDVDIFEINEAFASQAAYCVEKLRLPPEKVNPLGGAVALGHPLGCTGARQVITLLNELKRRGKRAYGVVSMCIGTGMGAAAVFEYPGN |
| 预测分子量 | 47.9 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3篇与thiO重组蛋白相关的文献摘要示例(注：文献内容为示例性概括，具体文献需根据实际检索结果确认)：
1. **文献名称**：*"Heterologous expression and characterization of ThiO, a thiamine-binding protein from Bacillus subtilis"*
**作者**：J. M. Smith et al.
**摘要**：研究报道了枯草芽孢杆菌来源的ThiO蛋白在大肠杆菌中的重组表达与纯化，证实其具有硫胺素结合活性，并解析了其底物特异性结构域。
2. **文献名称**：*"Functional analysis of ThiO in thiamine biosynthesis: Insights from recombinant enzyme kinetics"*
**作者**：L. Chen & R. Gupta
**摘要**：通过重组表达ThiO蛋白并分析其酶动力学，揭示了其在硫胺素生物合成途径中催化前体分子氧化的关键作用及辅因子依赖性。
3. **文献名称**：*"Crystal structure of recombinant ThiO from Saccharomyces cerevisiae and its role in antioxidant metabolism"*
**作者**：K. Tanaka et al.
**摘要**：解析了酵母ThiO重组蛋白的晶体结构，发现其参与调控细胞内氧化应激反应，并提出其可能作为硫代谢通路中的多功能酶。
如需具体文献，建议通过PubMed或Google Scholar以关键词“thiO recombinant protein”或“ThiO heterologous expression”检索最新研究。
**Background of thiO Recombinant Protein**
The thiO gene encodes a key enzyme involved in thiamine (vitamin B₁) biosynthesis, primarily studied in bacteria such as *Escherichia coli*. Thiamine is essential for cellular metabolism, acting as a cofactor in critical pathways like carbohydrate and amino acid metabolism. The thiO protein, a thiamine phosphate synthase, catalyzes the ATP-dependent phosphorylation of thiamine monophosphate (TMP) to form thiamine pyrophosphate (TPP), the active coenzyme form. This step is crucial for ensuring the bioavailability of TPP in organisms that synthesize thiamine de novo.
Recombinant thiO protein is produced through genetic engineering, where the thiO gene is cloned into expression vectors (e.g., plasmids) and expressed in heterologous hosts like *E. coli*. This allows large-scale production of the enzyme for structural, functional, and industrial studies. Purification techniques, such as affinity chromatography with His-tags, enable isolation of high-purity thiO for biochemical assays.
Research on thiO has provided insights into its enzymatic mechanism, substrate specificity, and regulatory roles in thiamine biosynthesis. Structural studies reveal conserved domains involved in ATP and TMP binding, aiding in understanding its catalytic activity. Additionally, thiO has been explored for biotechnological applications, including metabolic engineering to enhance thiamine production in microbes for nutritional supplements or industrial fermentation.
Mutations or dysregulation of thiO homologs in plants and pathogens highlight its broader biological significance, linking it to stress responses and pathogenicity. Overall, thiO recombinant protein serves as a valuable tool for both basic research and applied biotechnological innovations.
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