| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSD17B7 |
| Uniprot No | P56937 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-341aa |
| 氨基酸序列 | MRKVVLITGASSGIGLALCKRLLAEDDELHLCLACRNMSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQRLDCIYLNAGIMPNPQLNIKALFFGLFSRKVIHMFSTAEGLLTQGDKITADGLQEVFETNVFGHFILIRELEPLLCHSDNPSQLIWTSSRSARKSNFSLEDFQHSKGKEPYSSSKYATDLLSVALNRNFNQQGLYSNVACPGTALTNLTYGILPPFIWTLLMPAILLLRFFANAFTLTPYNGTEALVWLFHQKPESLNPLIKYLSATTGFGRNYIMTQKMDLDEDTAEKFYQKLLELEKHIRVTIQKTDNQARLSGSCL |
| 分子量 | 64.6 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篇关于重组人HSD17B7蛋白的参考文献示例(注：文献信息为模拟示例，实际引用需核实准确性)：
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1. **文献名称**：*"Functional characterization of recombinant human HSD17B7 as a 3-ketosteroid reductase in cholesterol biosynthesis"*
**作者**：S. Moeller et al.
**摘要**：研究通过昆虫细胞表达系统成功获得重组人HSD17B7蛋白，证实其催化3-酮类固醇转化为胆固醇前体的酶活性，揭示了其在胆固醇合成途径中的关键作用。
2. **文献名称**：*"Expression and enzymatic activity analysis of recombinant HSD17B7 in human cancer cell lines"*
**作者**：L. Chen et al.
**摘要**：利用哺乳动物细胞表达重组HSD17B7.发现其在乳腺癌细胞中通过调节雌酮/雌二醇代谢促进细胞增殖，为靶向治疗提供潜在依据。
3. **文献名称**：*"Structural basis for substrate specificity of human HSD17B7 in steroid metabolism"*
**作者**：T. Nakamura et al.
**摘要**：通过晶体结构解析和突变实验，阐明重组HSD17B7对类固醇底物的选择性机制，揭示了催化位点的关键氨基酸残基。
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如需实际文献，建议检索PubMed/Google Scholar并筛选近5年研究，重点关注表达系统、功能验证或疾病关联方向。
Human 17β-hydroxysteroid dehydrogenase type 7 (HSD17B7) is a member of the 17β-HSD enzyme family, which plays critical roles in steroid metabolism by interconverting active and inactive forms of sex steroids. Initially characterized as a prolactin receptor-associated protein (PARP), HSD17B7 primarily catalyzes the conversion of estrone to estradiol (a potent estrogen) and dihydrotestosterone to 5α-androstanediol, linking it to estrogen biosynthesis and androgen metabolism. It is expressed in steroidogenic tissues like ovaries, placenta, and breast, suggesting involvement in local hormone regulation.
Structurally, HSD17B7 contains a conserved Rossmann-fold domain typical of short-chain dehydrogenases/reductases (SDRs). Unlike other 17β-HSD isoforms, it localizes to the endoplasmic reticulum and requires NADPH/NADH as cofactors. Dysregulation of HSD17B7 has been implicated in hormone-dependent cancers (e.g., breast, ovarian) due to its role in modulating intracellular estrogen levels.
Recombinant human HSD17B7 protein is produced via heterologous expression systems (e.g., E. coli, mammalian cells) for functional studies. It serves as a tool to investigate enzymatic kinetics, substrate specificity, and inhibitor screening for therapeutic development. Researchers also explore its interaction with cellular pathways beyond steroidogenesis, including cholesterol biosynthesis, highlighting its multifaceted biological significance. Its recombinant form enables structural studies (e.g., crystallography) and drug discovery efforts targeting hormone-related disorders.
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