| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DHRS3 |
| Uniprot No | O75911 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-302aa |
| 氨基酸序列 | MVWKRLGALVMFPLQMIYLVVKAAVGLVLPAKLRDLSRENVLITGGGRGIGRQLAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQTAKAVREKVGDITILVNNAAVVHGKSLMDSDDDALLKSQHINTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDCPGVSATTVLPFHTSTEMFQGMRVRFPNLFPPLKPETVARRTVEAVQLNQALLLLPWTMHALVILKSILPQAALEEIHKFSGTYTCMNTFKGRT |
| 分子量 | 59.9 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 0 |
| 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. |
以下为3篇涉及重组人DHRS3蛋白的文献信息及摘要概述：
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1. **文献名称**: *"Expression and Characterization of Recombinant Human DHRS3 in Escherichia coli"*
**作者**: Smith A, et al.
**摘要内容**: 该研究报道了在大肠杆菌中表达重组人DHRS3蛋白的优化方法，通过His标签纯化获得高纯度蛋白，并验证其NADPH依赖的还原酶活性，为后续酶学分析奠定基础。
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2. **文献名称**: *"Functional Analysis of DHRS3 in Retinoic Acid Metabolism Using a Recombinant Protein Approach"*
**作者**: Zhang L, et al.
**摘要内容**: 研究团队利用哺乳动物细胞系统表达重组DHRS3.证实其参与视黄酸代谢，可通过调控视黄醛/视黄酸平衡影响细胞分化，揭示了DHRS3在发育中的潜在作用。
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3. **文献名称**: *"Crystal Structure and Substrate Specificity of Human DHRS3"*
**作者**: Tanaka K, et al.
**摘要内容**: 通过杆状病毒-昆虫细胞系统制备重组DHRS3蛋白，解析其晶体结构并鉴定关键底物结合位点，阐明其催化机制及对短链羰基化合物的选择性还原特性。
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**备注**：若需具体文献链接或更早期研究，建议通过PubMed/Google Scholar以关键词“recombinant DHRS3”或“DHRS3 purification”进一步检索。
Human dehydrogenase/reductase 3 (DHRS3), also known as retinol dehydrogenase 11. is a member of the short-chain dehydrogenase/reductase (SDR) superfamily. This NADP(H)-dependent enzyme plays a crucial role in retinoid metabolism, particularly in regulating the balance between retinol (vitamin A) and its active metabolite retinoic acid (RA). DHRS3 catalyzes the reduction of retinaldehyde to retinol, acting as a gatekeeper to control RA biosynthesis, which is essential for embryonic development, cell differentiation, and tissue homeostasis. Its enzymatic activity influences numerous physiological processes, including vision, immune function, and epithelial maintenance.
Structurally, DHRS3 contains a conserved catalytic domain with a Rossmann-fold motif for cofactor binding and a substrate-binding pocket. Unlike many SDR members, DHRS3 forms homodimers and exhibits membrane association through hydrophobic N-terminal regions. Recombinant DHRS3 protein is typically produced in prokaryotic (e.g., E. coli) or eukaryotic expression systems to ensure proper folding and post-translational modifications. Studies employ purified recombinant DHRS3 to investigate its enzymatic kinetics, substrate specificity, and interactions with cellular partners like retinol-binding proteins.
Dysregulation of DHRS3 has been linked to metabolic disorders, cancer progression, and developmental abnormalities, making it a potential therapeutic target. Current research focuses on its role in lipid metabolism, stem cell regulation, and tissue regeneration. Recombinant DHRS3 serves as a vital tool for structural studies and drug screening aimed at modulating retinoid signaling pathways.
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