| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | iolG |
| Uniprot No | P26935 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-344aa |
| 氨基酸序列 | MSLRIGVIGTGAIGKEHINRITNKLSGAEIVAVTDVNQEAAQKVVEQYQLNATVYPNDDSLLADENVDAVLVTSWGPAHESSVLKAIKAQKYVFCEKPLATTAEGCMRIVEEEIKVGKRLVQVGFMRRYDSGYVQLKEALDNHVIGEPLMIHCAHRNPTVGDNYTTDMAVVDTLVHEIDVLHWLVNDDYESVQVIYPKKSKNALPHLKDPQIVVIETKGGIVINAEIYVNCKYGYDIQCEIVGEDGIIKLPEPSSISLRKEGRFSTDILMDWQRRFVAAYDVEIQDFIDSIQKKGEVSGPTAWDGYIAAVTTDACVKAQESGQKEKVELKEKPEFYQSFTTVQN |
| 预测分子量 | 54.4 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iolG重组蛋白的3篇代表性文献的简要概括(注：文献信息为模拟示例，实际引用时请核实真实来源)：
1. **文献名称**：*Cloning and characterization of iolG from Bacillus subtilis: a key enzyme in myo-inositol catabolism*
**作者**：Smith A, et al.
**摘要**：该研究报道了枯草芽孢杆菌中iolG基因的克隆及在大肠杆菌中的重组表达，证实其编码的脱氢酶催化肌醇代谢的中间产物，并分析了重组蛋白的酶动力学参数。
2. **文献名称**：*Structural insights into the substrate specificity of IolG dehydrogenase through X-ray crystallography*
**作者**：Zhang L, et al.
**摘要**：通过X射线晶体学解析了重组IolG蛋白的三维结构，揭示了其底物结合口袋的关键氨基酸残基，阐明了其对肌醇衍生物的选择性催化机制。
3. **文献名称**：*Metabolic engineering of Escherichia coli using iolG for the production of scyllo-inositol*
**作者**：Tanaka K, et al.
**摘要**：研究利用重组IolG蛋白的脱氢酶活性，构建工程化大肠杆菌菌株，将葡萄糖转化为高附加值的scyllo-肌醇，验证了其在生物制造中的应用潜力。
4. **文献名称**：*Functional analysis of iolG in bacterial inositol utilization pathways*
**作者**：Wang Q, et al.
**摘要**：通过基因敲除和重组蛋白互补实验，证实iolG在细菌肌醇分解代谢中的必要性，并发现其表达受碳源调控，参与细胞内碳代谢平衡。
(提示：实际文献需通过PubMed/Google Scholar等平台以“iolG recombinant protein”、“IolG dehydrogenase”等关键词检索获取。)
**Background of iolG Recombinant Protein**
The iolG gene, primarily studied in *Bacillus subtilis* and related bacteria, encodes a key enzyme involved in inositol metabolism. Inositol, a cyclic sugar alcohol, serves as a carbon source for certain microorganisms, and its catabolism is mediated by the *iol* (inositol utilization) operon. iolG is annotated as a dehydrogenase responsible for converting *myo*-inositol into 2-deoxy-5-keto-*D*-gluconic acid, a critical step in the pathway that channels inositol into central metabolism. This enzyme plays a role in bacterial survival under nutrient-limiting conditions, particularly in environments where inositol is available as an energy source.
Recombinant iolG protein is produced via heterologous expression systems, such as *Escherichia coli*, enabling large-scale purification for biochemical and structural studies. Its recombinant form retains catalytic activity and stability, making it a valuable tool for exploring enzyme mechanisms, substrate specificity, and potential biotechnological applications. Studies on iolG have contributed to understanding microbial metabolic diversity, particularly in pathways linked to environmental adaptation and carbon-source utilization.
Additionally, iolG’s enzymatic properties are of interest in industrial biocatalysis, where it could be engineered for chiral compound synthesis or biofuel precursor production. Its role in inositol degradation also intersects with biomedical research, as inositol derivatives are involved in eukaryotic signaling pathways, suggesting potential cross-disciplinary relevance. Overall, iolG recombinant protein serves as a model for studying bacterial metabolism while offering avenues for applied enzymology and metabolic engineering.
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