| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PRAP1 |
| Uniprot No | Q96NZ9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-151aa |
| 氨基酸序列 | MRRLLLVTSL VVVLLWEAGA VPAPKVPIKM QVKHWPSEQD PEKAWGARVV EPPEKDDQLV VLFPVQKPK LLTTEEKPRG QGRGPILPGT KAWMETEDTL GHVLSPEPDH DSLYHPPPEE DQGEERPRL WVMPNHQVLL GPEEDQDHIY HPQ |
| 预测分子量 | 16 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PRAP1重组蛋白的3篇代表性文献摘要概括(注：文献为模拟示例，实际研究需根据具体数据库检索确认)：
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1. **文献名称**：*Expression and Functional Characterization of Recombinant PRAP1 Protein in Prostate Cancer Cells*
**作者**：Smith A, Johnson R, Lee C.
**摘要**：本研究利用大肠杆菌系统成功表达并纯化了PRAP1重组蛋白，验证其在体外促进前列腺癌细胞凋亡的功能。实验表明，PRAP1通过调节Bcl-2/Bax通路抑制肿瘤生长，提示其潜在治疗价值。
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2. **文献名称**：*PRAP1 Recombinant Protein Attenuates Oxidative Stress in Vascular Endothelial Cells*
**作者**：Wang Y, Chen L, Zhang H.
**摘要**：作者通过哺乳动物细胞表达系统制备了高活性的PRAP1重组蛋白，并发现其能显著减少内皮细胞中ROS水平，保护细胞免受氧化损伤。研究为心血管疾病治疗提供了新靶点。
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3. **文献名称**：*Development of a PRAP1-Based ELISA for Early Cancer Detection*
**作者**：Kim S, Gupta P, Martínez F.
**摘要**：该研究优化了PRAP1重组蛋白的昆虫杆状病毒表达工艺，并基于此开发了高灵敏度ELISA检测方法。临床样本分析显示，PRAP1在多种癌症患者血清中异常高表达，具备诊断潜力。
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如需进一步检索真实文献，建议使用PubMed或Web of Science平台，以“PRAP1 recombinant”或“PRAP1 protein expression”为关键词筛选。
PRAP1 (Prolactin Receptor-Associated Protein 1) is a protein encoded by the _PRAP1_ gene, initially identified for its interaction with the prolactin receptor (PRLR) and potential role in prolactin signaling pathways. Prolactin, a hormone primarily associated with lactation and reproductive functions, exerts its effects through PRLR-mediated signaling, influencing cell proliferation, differentiation, and survival. PRAP1 is thought to modulate these pathways, though its precise molecular mechanisms remain under investigation. Structurally, PRAP1 contains a conserved N-terminal domain and intrinsically disordered regions, suggesting roles in protein-protein interactions or scaffolding.
Recombinant PRAP1 protein, produced via expression systems like _E. coli_ or mammalian cells, enables functional studies to dissect its biological activities. Researchers employ it to explore its interaction partners, post-translational modifications, and regulatory effects on prolactin signaling. Emerging evidence links PRAP1 to cancer biology, particularly in hormone-responsive cancers (e.g., breast, ovarian), where aberrant prolactin signaling may drive tumor progression. Additionally, PRAP1 is implicated in placental development and maternal-fetal communication, highlighting its broader physiological relevance.
Despite progress, the protein’s full functional spectrum and disease associations remain unclear. Recombinant PRAP1 tools are critical for resolving these gaps, offering insights into its role in cellular homeostasis, endocrine regulation, and pathology. Such studies may pave the way for therapeutic strategies targeting PRAP1-PRLR interactions in cancer or reproductive disorders. Overall, PRAP1 represents a promising yet underexplored component of prolactin signaling, with recombinant protein technology serving as a key enabler for advancing its biomedical understanding.
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