| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PRLR |
| Uniprot No | P16471 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 25-234aa |
| 氨基酸序列 | QLPPGKPEIFKCRSPNKETFTCWWRPGTDGGLPTNYSLTYHREGETLMHECPDYITGGPNSCHFGKQYTSMWRTYIMMVNATNQMGSSFSDELYVDVTYIVQPDPPLELAVEVKQPEDRKPYLWIKWSPPTLIDLKTGWFTLLYEIRLKPEKAAEWEIHFAGQQTEFKILSLHPGQKYLVQVRCKPDHGYWSAWSPATFIQIPSDFTMND |
| 预测分子量 | 27.2 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PRLR重组蛋白的3篇文献概览(内容基于公开研究整理，非真实文献)：
1. **《重组人催乳素受体的表达及其与催乳素结合特性研究》**
*作者：Zhang et al.*
摘要：通过大肠杆菌系统成功表达并纯化PRLR胞外段重组蛋白，验证其与催乳素(PRL)的特异性结合能力，为PRL/PRLR信号通路研究提供工具。
2. **《PRLR重组蛋白的晶体结构解析与功能分析》**
*作者：Li et al.*
摘要：利用X射线晶体学解析PRLR重组蛋白的三维结构，揭示其与配体结合的关键结构域，并探讨突变对信号转导的影响。
3. **《PRLR重组蛋白在乳腺癌细胞增殖中的作用机制》**
*作者：Wang et al.*
摘要：通过体外实验证明PRLR重组蛋白可激活下游STAT5通路，促进乳腺癌细胞增殖，提示其作为治疗靶点的潜在价值。
4. **《基于昆虫细胞系统的PRLR重组蛋白规模化制备》**
*作者：Chen et al.*
摘要：优化杆状病毒-昆虫细胞表达系统，实现PRLR重组蛋白的高效分泌表达，为抗体药物筛选提供高纯度蛋白原料。
(注：以上为模拟文献，实际文献需通过PubMed、Web of Science等平台检索确认。)
The prolactin receptor (PRLR) is a transmembrane protein belonging to the class I cytokine receptor superfamily. It plays a critical role in mediating the biological effects of prolactin (PRL), a hormone essential for lactation, reproduction, immune regulation, and metabolism. PRLR activation triggers downstream signaling pathways, primarily JAK2-STAT5. regulating gene expression involved in cell proliferation, differentiation, and survival. Structurally, PRLR consists of an extracellular domain for ligand binding, a transmembrane helix, and an intracellular domain for signal transduction. Alternative splicing generates multiple isoforms with distinct functions, contributing to tissue-specific responses.
Recombinant PRLR proteins are engineered in vitro using expression systems like *E. coli*, mammalian cells, or insect cells to study receptor-ligand interactions, signaling mechanisms, and therapeutic applications. These proteins retain key functional domains, enabling researchers to investigate PRLR's role in diseases such as breast cancer, prostate cancer, and autoimmune disorders, where dysregulated PRL signaling is implicated. Recombinant PRLR also serves as a tool for drug screening, particularly for developing antagonists to block hyperactive PRLR pathways in oncology. Additionally, it aids in structural studies (e.g., crystallography) to map binding sites and design targeted therapies. Despite challenges like protein solubility and post-translational modification fidelity, advancements in recombinant technology continue to enhance its utility in both basic research and clinical translation.
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