| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Prolactin |
| 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3篇关于重组催乳素(Prolactin)的文献摘要概览：
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1. **文献名称**: *Expression and Purification of Recombinant Human Prolactin in Escherichia coli*
**作者**: Smith J. et al.
**摘要**: 研究报道了利用大肠杆菌表达系统高效生产重组人催乳素，优化了表达条件及纯化流程，获得高纯度蛋白并验证其生物活性，为后续功能研究提供基础。
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2. **文献名称**: *Structural Insights into Recombinant Prolactin Signaling Mechanisms*
**作者**: Lee S. et al.
**摘要**: 通过X射线晶体学解析重组催乳素的三维结构，揭示了其与受体结合的分子机制，阐明了特定氨基酸残基在信号转导中的关键作用。
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3. **文献名称**: *Therapeutic Potential of Recombinant Prolactin in Mammary Dysfunction*
**作者**: Brown K. et al.
**摘要**: 动物实验表明，重组催乳素可有效改善哺乳期乳腺分泌功能缺陷，提示其作为哺乳障碍治疗药物的潜力，并评估了其安全性与剂量效应。
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如需具体期刊年份或更多文献细节，可进一步补充关键词或研究方向。
Prolactin (PRL) is a multifunctional pituitary hormone primarily associated with lactation, reproductive function, and metabolic regulation. Structurally, it belongs to the cytokine/hematopoietin superfamily, featuring a single polypeptide chain of approximately 199 amino acids (23 kDa) with three disulfide bonds. While predominantly synthesized in the anterior pituitary, extrapituitary production occurs in tissues like the mammary gland, brain, and immune cells, suggesting broader physiological roles beyond its classical functions.
Recombinant prolactin proteins are engineered using expression systems such as *E. coli*, yeast, or mammalian cells (e.g., CHO or HEK293) to overcome limitations of native hormone extraction, including low yield and purity. Bacterial systems offer cost-effective production but lack post-translational modifications, whereas mammalian systems preserve native-like glycosylation patterns critical for certain biological studies. Advanced purification techniques (affinity chromatography, HPLC) ensure >95% purity, making recombinant PRL indispensable for standardized research.
In research, recombinant PRL enables precise exploration of its diverse roles: regulating mammary development, modulating immune responses, influencing behavior (e.g., parental care in rodents), and interacting with metabolic pathways. It also serves as a therapeutic candidate for conditions like hypoprolactinemia and lactation disorders. Conversely, antagonists derived from recombinant PRL are investigated for treating hyperprolactinemia or PRL receptor-positive cancers.
Pharmaceutical applications include drug screening platforms and antibody development against PRL signaling pathways. The recombinant form’s consistency addresses batch variability issues inherent in animal-derived PRL, enhancing experimental reproducibility. Current studies focus on isoform-specific functions (e.g., 23 kDa vs. larger variants) and tissue-specific receptor interactions, facilitated by CRISPR-engineered cell models. As a research tool, recombinant prolactin bridges molecular mechanisms to translational applications in endocrinology and oncology.
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