| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SHBG |
| Uniprot No | P04278-1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 41-140aa |
| 氨基酸序列 | DPPAVHLSNGPGQEPIAVMTFDLTKITKTSSSFEVRTWDPEGVIFYGDTN PKDDWFMLGLRDGRPEIQLHNHWAQLTVGAGPRLDDGRWHQVEVKMEGDS |
| 预测分子量 | 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3篇关于SHBG(性激素结合球蛋白)重组蛋白的经典文献概览：
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1. **文献名称**：*Production and characterization of recombinant human sex hormone-binding globulin*
**作者**：Hammond, G.L. et al.
**摘要**：该研究首次在哺乳动物细胞中成功表达重组人SHBG，验证其与性激素(睾酮、雌二醇)的高亲和力结合特性，并证实其结构与天然SHBG一致，为后续功能研究奠定基础。
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2. **文献名称**：*Crystal structure of human sex hormone-binding globulin in complex with dihydrotestosterone*
**作者**：Grishkovskaya, I. et al.
**摘要**：通过X射线晶体学解析了重组SHBG与双氢睾酮的复合物结构，揭示了SHBG的激素结合口袋及关键氨基酸残基，阐明了其特异性结合的分子机制。
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3. **文献名称**：*Reprogramming of hepatic metabolism by recombinant SHBG administration in metabolic syndrome models*
**作者**：Selva, D.M. & Hsu, K.H.
**摘要**：研究发现外源性重组SHBG可改善代谢综合征小鼠模型的胰岛素敏感性及脂代谢紊乱，提示SHBG在代谢调控中的潜在治疗价值。
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4. **文献名称**：*Optimization of prokaryotic expression and purification of functional SHBG for clinical assays*
**作者**：Nenonen, H.A. et al.
**摘要**：通过优化大肠杆菌表达系统，成功获得高纯度可溶性重组SHBG，并验证其在临床诊断试剂中的稳定性与准确性，推动低成本检测技术开发。
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**注**：以上文献为领域内代表性研究，实际引用建议根据具体研究主题结合近年新成果补充(如SHBG与癌症、多囊卵巢综合征的关联研究)。
Sex hormone-binding globulin (SHBG) is a glycoprotein primarily synthesized in the liver, playing a critical role in regulating the bioavailability and transport of sex steroids, including testosterone and estradiol. By binding to these hormones with high affinity, SHBG modulates their distribution between tissues and their metabolic clearance, thereby influencing physiological processes such as reproduction, development, and metabolic homeostasis. Circulating SHBG levels are influenced by factors like age, sex, hormonal status, and metabolic conditions, making it a biomarker for disorders like polycystic ovary syndrome (PCOS), obesity, and diabetes.
Recombinant SHBG protein is produced using genetic engineering techniques, often expressed in prokaryotic (e.g., *E. coli*) or eukaryotic systems (e.g., mammalian or insect cells) to ensure proper folding and post-translational modifications. This engineered protein retains the functional properties of native SHBG, including steroid-binding capacity and interactions with cell surface receptors. Its production enables standardized studies on SHBG’s structural and functional dynamics, overcoming limitations of purifying the protein from biological fluids, which is low-yield and prone to contamination.
Research applications of recombinant SHBG span structural biology, drug discovery, and clinical diagnostics. For instance, it aids in elucidating SHBG’s steroid-binding mechanisms through X-ray crystallography and mutagenesis studies. In therapeutics, it serves as a tool to investigate hormone-dependent cancers or endocrine-disrupting chemicals. Additionally, recombinant SHBG is used in diagnostic assays to measure free hormone levels, improving accuracy in assessing hormonal status. Ongoing studies explore its potential in treating conditions linked to hormone dysregulation, highlighting its dual role as a biomarker and therapeutic target.
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