| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | iolO |
| Uniprot No | Q9WYP7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-270aa |
| 氨基酸序列 | MKLSLVISTSDAAFDALAFKGDLRKGMELAKRVGYQAVEIAVRDPSIVDWNEVKILSEELNLPICAIGTGQAYLADGLSLTHPNDEIRKKAIERVVKHTEVAGMFGALVIIGLVRGRREGRSYEETEELFIESMKRLLELTEHAKFVIEPLNRYETDFINTIDDALRILRKINSNRVGILADTFHMNIEEVNIPESLKRAGEKLYHFHVADSNRWAPGCGHFDFRSVFNTLKEIGYNRYVSVECLPLPGGMEEAAEIAFKTLKELIIKLT |
| 预测分子量 | 37.9 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. |
以下是关于iolO重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：*Functional characterization of the iolO gene involved in inositol catabolism in *Bacillus subtilis***
**作者**：Yasutake, Y., et al.
**摘要**：该研究鉴定了枯草芽孢杆菌中iolO基因的功能，发现其编码一种肌醇代谢相关的脱氢酶。通过重组表达iolO蛋白并纯化，证实其在肌醇转化为葡萄糖代谢中间产物中的关键作用，揭示了该酶的底物特异性及催化机制。
2. **文献名称**：*Crystal structure and biochemical analysis of iolO from *Bacillus subtilis*: A novel enzyme in myo-inositol degradation pathway*
**作者**：Zhang, L., et al.
**摘要**：本研究解析了枯草芽孢杆菌iolO重组蛋白的晶体结构，结合酶活实验，发现iolO通过独特的催化结构域将肌醇转化为D-葡萄糖酸-1.5-内酯，为理解细菌肌醇代谢途径的分子机制提供了结构基础。
3. **文献名称**：*Heterologous expression and characterization of iolO as a potential biocatalyst in industrial applications*
**作者**：Chen, H., et al.
**摘要**：作者在大肠杆菌中异源表达了iolO重组蛋白，并优化其可溶性表达条件。功能研究表明，该酶在宽温度和pH范围内具有高稳定性，提示其在生物催化及工业手性化合物合成中的应用潜力。
(注：以上文献信息为示例性概括，实际文献需根据具体数据库检索结果确认。)
**Background of iolO Recombinant Protein**
The iolO recombinant protein is derived from the *iolO* gene, which is part of the *iol* (*inositol utilization*) operon in certain bacteria, notably *Bacillus subtilis*. This operon encodes enzymes involved in the catabolism of myo-inositol, a cyclic sugar alcohol, which serves as a carbon source under specific metabolic conditions. The *iolO* gene product, IolO, functions as a key enzyme in this pathway, specifically as a dehydrogenase or oxidase, facilitating the conversion of intermediates like 2-keto-myo-inositol into downstream metabolites.
Recombinant iolO protein is typically produced via heterologous expression in *Escherichia coli* or other host systems, enabling large-scale purification for biochemical and structural studies. Its production leverages genetic engineering to clone the *iolO* sequence into expression vectors, followed by induction with IPTG or similar agents. The purified protein is often studied for its enzymatic kinetics, substrate specificity, and role in bacterial inositol metabolism.
Research on iolO has implications for understanding microbial metabolic adaptation, particularly in environments where inositol is a primary carbon source. Additionally, the enzyme’s potential applications include biocatalysis for producing chiral intermediates in pharmaceutical synthesis or as a tool in metabolic engineering. Structural studies of iolO, including its cofactor-binding domains (e.g., FAD or NAD+ dependence), provide insights into its mechanism and evolutionary relationships with analogous enzymes in other organisms.
Overall, iolO recombinant protein serves as a model for studying bacterial carbohydrate metabolism and offers practical utility in biotechnology, emphasizing the intersection of microbial physiology and industrial enzymology.
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