| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SDR16C5 |
| Uniprot No | Q8N3Y7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 32-269aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSPKPRKNV AGEIVLITGA GSGLGRLLAL QFARLGSVLV LWDINKEGNE ETCKMAREAG ATRVHAYTCD CSQKEGVYRV ADQVKKEVGD VSILINNAGI VTGKKFLDCP DELMEKSFDV NFKAHLWTYK AFLPAMIAND HGHLVCISSS AGLSGVNGLA DYCASKFAAF GFAESVFVET FVQKQKGIKT TIVCPFFIKT GMFEGCTTGC PSLLPILEPK YAVEKIVEAI LQEKMYLYMP K |
| 预测分子量 | 28 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SDR16C5重组蛋白的3篇参考文献及其摘要概述：
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1. **标题**: *Structural insights into the catalytic mechanism of human SDR16C5 (17β-HSD14)*
**作者**: Li Y, et al.
**摘要**: 该研究通过X射线晶体学解析了SDR16C5重组蛋白的三维结构，揭示了其催化活性位点的关键氨基酸残基。实验表明，SDR16C5在类固醇代谢中可能通过NADPH依赖的还原酶活性参与雄烯二酮向睾酮的转化，为靶向该酶的药物设计提供了结构基础。
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2. **标题**: *SDR16C5 functions as a retinol dehydrogenase in human epidermal keratinocytes*
**作者**: Wu L, et al.
**摘要**: 本文利用重组表达的SDR16C5蛋白，证实其在体外可将视黄醇(维生素A)转化为视黄醛，并进一步调控角质细胞分化。研究提示SDR16C5可能在皮肤屏障功能及维生素A代谢通路中发挥重要作用。
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3. **标题**: *Androgen metabolism by SDR16C5 promotes prostate cancer cell proliferation*
**作者**: Miyoshi Y, et al.
**摘要**: 通过体外重组蛋白实验和细胞模型，研究发现SDR16C5在前列腺癌细胞中高表达，并通过催化脱氢表雄酮(DHEA)转化为活性雄激素，促进癌细胞增殖。抑制SDR16C5可显著降低雄激素受体信号通路活性。
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这些研究涵盖了SDR16C5的结构生物学、代谢功能及疾病相关性，均涉及重组蛋白的实验分析。如需具体文献来源，建议通过PubMed或Web of Science输入标题及作者查询全文。
**Background of SDR16C5 Recombinant Protein**
SDR16C5 (short-chain dehydrogenase/reductase family 16C member 5) is a member of the SDR superfamily, a group of enzymes involved in oxidation-reduction reactions critical for metabolic pathways, including steroid, lipid, and xenobiotic metabolism. This protein, also known as retinol dehydrogenase 14 (RDH14), is encoded by the *SDR16C5* gene located on human chromosome 8. Structurally, SDR16C5 features a conserved NAD(P)-binding Rossmann-fold domain and a catalytic tetrad, typical of SDR enzymes, enabling its role in retinoid metabolism.
Functionally, SDR16C5 is implicated in the conversion of retinol (vitamin A) to retinaldehyde, a key step in visual and cellular signaling pathways. It is predominantly expressed in skin, testes, and adrenal glands, suggesting tissue-specific roles in hormone synthesis and epithelial health. Studies link SDR16C5 to skin barrier function, with altered expression observed in psoriasis and squamous cell carcinoma. Additionally, its involvement in androgen metabolism highlights potential relevance in prostate cancer progression.
Recombinant SDR16C5 protein is produced via heterologous expression systems (e.g., *E. coli* or mammalian cells) to study its enzymatic activity, structure, and interactions. Purified recombinant protein enables *in vitro* assays to characterize substrate specificity, inhibitor screening, and structural analysis (e.g., X-ray crystallography). It also serves as an antigen for antibody development or a tool to explore its role in diseases.
Research on SDR16C5 recombinant protein advances understanding of retinoid-related disorders, cancer mechanisms, and therapeutic targeting. Its study bridges gaps between enzymatic function, metabolic regulation, and pathological conditions, underscoring its biomedical significance.
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