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纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | Prl |
Uniprot No | P33993 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-389aa |
氨基酸序列 | MALKDYALEKEKVKKFLQEFYQDDELGKKQFKYGNQLVRLAHREQVALYV DLDDVAEDDPELVDSICENARRYAKLFADAVQELLPQYKEREVVNKDVLD VYIEHRLMMEQRSRDPGMVRSPQNQYPAELMRRFELYFQGPSSSKPRVIR EVRADSVGKLVTVRGIVTRVSEVKPKMVVATYTCDQCGAETYQPIQSPTF MPLIMCPSQECQTNRSGGRLYLQTRGSRFIKFQEMKMQEHSDQVPVGNIP RSITVLVEGENTRIAQPGDHVSVTGIFLPILRTGFRQVVQGLLSETYLEA HRIVKMNKSEDDESGAGELTREELRQIADVIFATVRELVSGGRSVRFSEA EQRCVSRGFTPAQFQAALDEYEELNVWQVNASRTRITFV |
预测分子量 | 69 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. |
以下是关于重组催乳素(Prl)蛋白的3篇代表性文献及其摘要概述:
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1. **文献名称**:*High-level expression and purification of biologically active recombinant human prolactin in Escherichia coli*
**作者**:Smith, J., et al.
**摘要**:研究报道了一种利用大肠杆菌高效表达并纯化具有生物活性的人源重组催乳素的方法,通过密码子优化和诱导条件调控显著提高了蛋白产量,纯化产物在体外细胞实验中展现出与天然催乳素相似的受体激活能力。
2. **文献名称**:*Structural analysis of recombinant murine prolactin and its receptor binding mechanism*
**作者**:Lee, S., et al.
**摘要**:通过哺乳动物细胞系统表达重组小鼠催乳素,结合X射线晶体学与分子对接技术解析其三维结构,揭示了催乳素与受体结合的关键氨基酸残基,为靶向药物设计提供了结构基础。
3. **文献名称**:*Functional characterization of recombinant porcine prolactin produced in Pichia pastoris for agricultural applications*
**作者**:Zhang, Y., et al.
**摘要**:开发了一种基于毕赤酵母的重组猪催乳素生产平台,优化发酵工艺后获得高纯度蛋白,实验证实其可显著提高哺乳期母猪的泌乳量,表明其在畜牧业中的潜在应用价值。
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**说明**:以上文献为示例,实际引用时需核实具体作者、期刊及发表年份。若需扩展,可关注催乳素在疾病模型(如乳腺癌)或新型表达系统(如植物表达体系)中的研究。
**Background of Prl Recombinant Protein**
Prolactin (Prl), a peptide hormone primarily secreted by the anterior pituitary gland, plays diverse roles in physiological processes, including lactation, reproduction, metabolism, and immune regulation. Initially identified for its critical function in mammary gland development and milk production, Prl has since been recognized as a multifunctional cytokine with receptors widely distributed across tissues. Its structure comprises a single polypeptide chain of approximately 199 amino acids, stabilized by three disulfide bonds, and shares structural homology with growth hormone and placental lactogen.
The advent of recombinant DNA technology in the late 20th century enabled the production of Prl as a recombinant protein (rhPrl), bypassing the need for extraction from animal or human sources. Recombinant Prl is typically synthesized using prokaryotic (e.g., *E. coli*) or eukaryotic (e.g., mammalian cell lines) expression systems. Eukaryotic systems are preferred for generating properly folded, post-translationally modified variants, crucial for functional studies.
Recombinant Prl has become a vital tool in biomedical research, facilitating studies on its signaling pathways, receptor interactions, and roles in diseases such as hyperprolactinemia, infertility, and cancer. It also holds therapeutic potential, particularly in addressing lactation disorders or as a component of regenerative therapies. However, challenges remain in optimizing production yield, stability, and bioactivity.
Current research focuses on engineering Prl analogs with enhanced specificity or modified functions, leveraging structural biology insights. Additionally, recombinant Prl is increasingly used in diagnostics and as a reference standard in immunoassays. As understanding of its pleiotropic actions expands, recombinant Prl continues to bridge basic science and clinical applications, underscoring its importance in endocrinology and biotechnology.
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