| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LHB |
| Uniprot No | A7Y161 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-201aa |
| 氨基酸序列 | GLLLLLLLSMGGAWASREPLRPWCHPINAILAVEKEGCPVCITVNTTICAGYCPTMLSCLGPGADAATSGPDPQRQRGRKGGLPLWPAVGEWGVGRQEQRASWAPESRTCGVSLGAQLRRWPQAHAHSPTHTASRCACCRRSCRPCLRWCAPTVMCASSPSGSLAARVVWTPWSPSLWLSAVAVDPAAAAPLTVGVPKTTP |
| 预测分子量 | 21,2 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LHB(Luteinizing Hormone Beta-subunit)重组蛋白研究的3篇示例文献(内容为示例，建议通过学术数据库核实最新研究)：
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1. **文献名称**：*Expression and characterization of recombinant human luteinizing hormone (LH) in Chinese hamster ovary cells*
**作者**：Smith A, et al.
**摘要**：本研究利用CHO细胞表达系统成功表达了具有生物活性的重组人LHB蛋白，并通过质谱和ELISA验证其结构完整性。实验表明，重组LHB与α亚基结合后可激活LH受体，为生殖激素替代疗法提供了潜在候选药物。
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2. **文献名称**：*Optimization of LHB protein production in E. coli using codon bias adjustment*
**作者**：Zhang L, et al.
**摘要**：通过优化大肠杆菌的密码子偏好性，显著提高了重组LHB蛋白的可溶性表达。纯化后的蛋白在体外实验中显示出与天然LH相似的激素活性，为低成本大规模生产LHB提供了新策略。
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3. **文献名称**：*Structural and functional analysis of glycosylated LHB variants*
**作者**：Johnson R, et al.
**摘要**：本研究对比了不同糖基化修饰的重组LHB蛋白，发现特定糖链结构可延长其在体内的半衰期并增强受体结合效率，揭示了糖基化对LHB功能调控的关键作用。
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**建议**：通过PubMed(https://pubmed.ncbi.nlm.nih.gov)或Google Scholar搜索关键词“recombinant LHB protein”、“luteinizing hormone beta subunit expression”获取最新研究进展。
**Background of LHB Recombinant Protein**
Luteinizing hormone (LH) is a glycoprotein hormone critical for regulating reproductive functions in mammals. It consists of two subunits: α (common to other glycoprotein hormones like FSH and TSH) and β (LHB), which confers biological specificity. Recombinant LHB protein refers to the beta subunit produced via recombinant DNA technology, enabling precise, scalable, and standardized synthesis without relying on animal-derived sources.
The development of recombinant LHB emerged from advancements in molecular biology and biopharmaceutical engineering in the late 20th century. Traditional LH extraction from animal or human sources faced challenges, including batch variability, ethical concerns, and contamination risks. Recombinant technology addressed these by expressing the LHB gene in host systems (e.g., CHO or HEK293 cells), ensuring high purity, consistency, and reduced immunogenicity.
LHB plays a pivotal role in LH's function, binding to luteinizing hormone receptors (LHR) in gonads to trigger steroidogenesis, ovulation, and gamete maturation. Recombinant LHB is instrumental in studying LH-LHR interactions, reproductive disorders (e.g., infertility, hypogonadism), and developing therapies. It also serves as a critical component in diagnostic assays and hormone replacement therapies.
In research, recombinant LHB facilitates structure-function studies, aiding in the design of analogs or antagonists for conditions like precocious puberty or hormone-dependent cancers. Its application extends to veterinary medicine and assisted reproductive technologies (ART).
Despite its advantages, challenges remain, such as optimizing post-translational modifications (e.g., glycosylation) to mimic native LH activity. Ongoing innovations in protein engineering and expression systems continue to enhance recombinant LHB's clinical and industrial relevance, solidifying its role in both basic science and translational medicine.
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