| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | Testo |
| Uniprot No | V6C9W4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-10aa |
| 氨基酸序列 | ANDERFALAA |
| 预测分子量 | 1.0 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. |
以下是关于睾酮(Testosterone)重组蛋白研究的虚构参考文献示例(注：以下内容为模拟生成，非真实文献)：
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1. **文献名称**: "Expression and Purification of Recombinant Human Testosterone-Binding Globulin in E. coli"
**作者**: Zhang, L.; et al.
**摘要**: 本研究通过大肠杆菌表达系统成功克隆并表达了人睾酮结合球蛋白(TeBG)的重组蛋白。通过优化诱导条件及亲和层析纯化，获得了高纯度蛋白。体外实验表明，重组TeBG对睾酮具有特异性结合能力，为激素运输机制研究提供了工具。
2. **文献名称**: "Structural Characterization of Recombinant Testosterone 17β-Dehydrogenase from Rat Liver"
**作者**: Tanaka, K.; et al.
**摘要**: 利用杆状病毒-昆虫细胞系统表达了大鼠睾酮17β-脱氢酶(17β-HSD)重组蛋白，并通过X射线晶体学解析了其三维结构。研究揭示了该酶催化睾酮与雄烯二酮相互转化的活性位点特征，为靶向抑制剂设计奠定基础。
3. **文献名称**: "Development of a Recombinant CYP3A4 Enzyme for In Vitro Testosterone Metabolism Studies"
**作者**: Müller, R.; et al.
**摘要**: 构建了重组人细胞色素P450 3A4(CYP3A4)的真核表达体系，验证了其对睾酮的6β-羟基化代谢活性。该重组酶可用于药物-激素相互作用的高通量筛选，替代传统肝微粒体模型。
4. **文献名称**: "Functional Analysis of Recombinant Androgen Receptor Ligand-Binding Domain in Hormone Therapy Research"
**作者**: Gupta, S.; et al.
**摘要**: 通过哺乳动物细胞表达并纯化了人雄激素受体(AR)的重组配体结合域(LBD)。表面等离子体共振(SPR)实验证实其与睾酮及合成类似物的结合动力学差异，为前列腺癌治疗药物开发提供数据支持。
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注：以上文献信息为模拟生成，实际研究中建议通过PubMed、Web of Science等平台检索真实文献。
Testo recombinant protein, typically referring to recombinant testosterone or testosterone-related proteins, is engineered using recombinant DNA technology to mimic the structure and function of endogenous testosterone. Testosterone, a primary male sex hormone, plays critical roles in reproductive health, muscle development, bone density, and metabolic regulation. Traditional testosterone therapies often rely on synthetic derivatives or animal-derived hormones, which may pose risks of immunogenicity, ethical concerns, or inconsistent bioavailability. Recombinant technology addresses these limitations by expressing the testosterone gene in microbial or mammalian host systems (e.g., E. coli, yeast, or CHO cells), enabling scalable, cost-effective production with high purity and batch-to-batch consistency.
The development of Testo recombinant protein aligns with advancements in biopharmaceuticals, particularly in hormone replacement therapies (HRT) for hypogonadism, gender-affirming care, and age-related testosterone deficiency. Its recombinant nature ensures reduced contamination risks compared to conventional extraction methods, while precise engineering allows customization (e.g., fusion tags for purification or extended half-life). Quality control involves rigorous assays (e.g., SDS-PAGE, Western blot, LC-MS) to confirm structural integrity and bioactivity via receptor-binding or cell-based assays.
Beyond therapeutics, Testo recombinant protein serves as a research tool for studying androgen receptor signaling, endocrine disorders, and metabolic pathways. It also supports diagnostic kit development for hormone level monitoring. Challenges remain in optimizing post-translational modifications (e.g., glycosylation) in prokaryotic systems and balancing bioactivity with stability. Nonetheless, its versatility and safety profile position it as a pivotal innovation in both clinical and biotechnological landscapes, reflecting the broader shift toward precision-engineered biologics.
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