| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | hdhA |
| Uniprot No | P0AET9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-255aa |
| 氨基酸序列 | MFNSDNLRLDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQLGGQAFACRCDITSEQELSALADFAISKLGKVDILVNNAGGGGPKPFDMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSYASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTDALKSVITPEIEQKMLQHTPIRRLGQPQDIANAALFLCSPAASWVSGQILTVSGGGVQELN |
| 预测分子量 | 34.2 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hdhA重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*Cloning, expression, and characterization of the hdhA gene encoding a thermostable 3-hydroxyacyl-CoA dehydrogenase from *Thermus thermophilus* HB8*
**作者**：Tanaka T, et al.
**摘要**：该研究报道了从嗜热菌 *Thermus thermophilus* 中克隆hdhA基因，并在大肠杆菌中高效表达重组蛋白。纯化后的酶显示出高热稳定性(最适温度75℃)，并证实其催化3-羟基酰基-CoA脱氢反应的活性，为工业生物催化提供潜在应用。
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2. **文献名称**：*Functional analysis of hdhA in *Bacillus subtilis*: Role in butanol tolerance and metabolism*
**作者**：Li Y, et al.
**摘要**：通过构建hdhA重组蛋白并分析其在枯草芽孢杆菌中的功能，发现hdhA编码的脱氢酶参与丁醇代谢途径，敲除该基因导致菌株丁醇耐受性显著下降，提示其在生物燃料生产中的调控作用。
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3. **文献名称**：*Crystal structure of recombinant hdhA from *Pseudomonas putida* reveals novel substrate binding motifs*
**作者**：Zhang R, et al.
**摘要**：本研究解析了恶臭假单胞菌hdhA重组蛋白的晶体结构(2.1Å分辨率)，发现其底物结合口袋具有独特的疏水氨基酸排列，解释了其对长链羟基酰基-CoA的特异性，为理性设计酶突变体奠定结构基础。
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**备注**：若需获取全文链接或补充文献，可提供更具体的领域关键词(如物种、应用方向等)。
**Background of hdhA Recombinant Protein**
The hdhA gene encodes a hydroxysteroid dehydrogenase (HSD), an enzyme involved in the metabolism of steroid compounds, particularly bile acids and cholesterol derivatives. This gene is notably found in certain pathogenic bacteria, such as *Clostridium difficile*, where it plays a critical role in modifying host-derived steroids to support microbial survival and virulence within the gut environment. By catalyzing the oxidation or reduction of hydroxyl groups on steroid molecules, HdhA helps bacteria evade host immune responses and adapt to the dynamic conditions of the gastrointestinal tract.
Interest in hdhA recombinant protein stems from its potential applications in both basic research and biotechnology. Structurally, HdhA belongs to the short-chain dehydrogenase/reductase (SDR) superfamily, characterized by a conserved Rossmann fold for cofactor binding (e.g., NAD+/NADP+). Recombinant versions of HdhA are typically produced via heterologous expression in *E. coli*, enabling detailed biochemical and structural studies. These studies aim to elucidate substrate specificity, catalytic mechanisms, and interactions with inhibitors, which could inform drug development targeting HdhA in pathogenic species.
Additionally, HdhA has garnered attention for its biotechnological utility in steroid biotransformation. Engineered HdhA variants could offer sustainable routes for synthesizing pharmaceutical steroids or degrading environmental pollutants. Its role in bacterial pathogenesis also positions it as a potential biomarker or therapeutic target for infections like *C. difficile*-associated diarrhea. Overall, hdhA recombinant protein serves as a versatile tool for exploring microbial metabolism, host-pathogen interactions, and enzyme-driven synthetic biology applications.
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