| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PGR |
| Uniprot No | P06401 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-933aa |
| 氨基酸序列 | MTELKAKGPRAPHVAGGPPSPEVGSPLLCRPAAGPFPGSQTSDTLPEVSAIPISLDGLLFPRPCQGQDPSDEKTQDQQSLSDVEGAYSRAEATRGAGGSSSSPPEKDSGLLDSVLDTLLAPSGPGQSQPSPPACEVTSSWCLFGPELPEDPPAAPATQRVLSPLMSRSGCKVGDSSGTAAAHKVLPRGLSPARQLLLPASESPHWSGAPVKPSPQAAAVEVEEEDGSESEESAGPLLKGKPRALGGAAAGGGAAAVPPGAAAGGVALVPKEDSRFSAPRVALVEQDAPMAPGRSPLATTVMDFIHVPILPLNHALLAARTRQLLEDESYDGGAGAASAFAPPRSSPCASSTPVAVGDFPDCAYPPDAEPKDDAYPLYSDFQPPALKIKEEEEGAEASARSPRSYLVAGANPAAFPDFPLGPPPPLPPRATPSRPGEAAVTAAPASASVSSASSSGSTLECILYKAEGAPPQQGPFAPPPCKAPGASGCLLPRDGLPSTSASAAAAGAAPALYPALGLNGLPQLGYQAAVLKEGLPQVYPPYLNYLRPDSEASQSPQYSFESLPQKICLICGDEASGCHYGVLTCGSCKVFFKRAMEGQHNYLCAGRNDCIVDKIRRKNCPACRLRKCCQAGMVLGGRKFKKFNKVRVVRALDAVALPQPVGVPNESQALSQRFTFSPGQDIQLIPPLINLLMSIEPDVIYAGHDNTKPDTSSSLLTSLNQLGERQLLSVVKWSKSLPGFRNLHIDDQITLIQYSWMSLMVFGLGWRSYKHVSGQMLYFAPDLILNEQRMKESSFYSLCLTMWQIPQEFVKLQVSQEEFLCMKVLLLLNTIPLEGLRSQTQFEEMRSSYIRELIKAIGLRQKGVVSSSQRFYQLTKLLDNLHDLVKQLHLYCLNTFIQSRALSVEFPEMMSEVIAAQLPKILAGMVKPLLFHKK |
| 预测分子量 | 98,9 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PGR重组蛋白的参考文献示例，涵盖不同研究领域：
1. **文献名称**: *"Recombinant Expression and Functional Analysis of PGRMC1 in Hormone-Dependent Cancer Cells*
**作者**: Johnson, R. et al. (2018)
**摘要**: 本研究通过大肠杆菌系统成功表达了重组人源PGRMC1(孕酮受体膜组分1)，并发现其在乳腺癌细胞中调控雌激素信号通路，影响细胞增殖和凋亡，为靶向治疗提供新思路。
2. **文献名称**: *"Heterologous Production of PGR5 Protein and Its Role in Photosynthetic Electron Transport*
**作者**: Tanaka, K. et al. (2016)
**摘要**: 在拟南芥中重组表达的PGR5蛋白被证实通过调控循环电子传递链增强光系统I的活性，提高了植物在强光胁迫下的光保护能力。
3. **文献名称**: *"A Recombinant Plant Growth-Regulating Protein Enhances Drought Tolerance in Oryza sativa*
**作者**: Chen, L. et al. (2020)
**摘要**: 利用植物表达系统生产的重组PGR蛋白(OsPGR1)显著促进水稻根系发育，并通过激活抗氧化酶系统提升植株的耐旱性，为农业应用提供潜在工具。
4. **文献名称**: *"Structural and Biochemical Characterization of a Recombinant PGR Protein from Glycine max*
**作者**: Park, S. et al. (2019)
**摘要**: 通过X射线晶体学解析了大豆来源的重组PGR蛋白三维结构，揭示其与植物激素结合的活性位点，为设计新型生长调节剂奠定基础。
**注**：以上文献为示例，具体研究需根据实际发表的论文调整。PGR在不同领域可能指代不同蛋白(如植物生长调节蛋白或孕酮受体相关蛋白)，建议结合研究方向进一步筛选文献。
**Background of PGR Recombinant Protein**
PGR (Progesterone Receptor) recombinant protein is a engineered form of the nuclear hormone receptor critical for mediating progesterone signaling, which regulates reproductive functions, embryonic development, and cellular homeostasis. Native PGR exists as two isoforms (PGR-A and PGR-B), derived from alternative splicing, and acts as a ligand-activated transcription factor. Dysregulation of PGR is linked to reproductive disorders, cancers, and metabolic conditions, driving interest in recombinant PGR for research and therapeutic applications.
Recombinant PGR is typically produced using heterologous expression systems (e.g., *E. coli*, insect, or mammalian cells*), enabling large-scale purification of functional protein. These systems allow precise control over post-translational modifications, enhancing protein stability and activity. The recombinant form retains progesterone-binding capacity and DNA interaction domains, facilitating structural studies, drug screening, and mechanistic insights into hormone-receptor interactions.
In biomedical research, PGR recombinant protein is utilized to investigate progesterone’s role in endometriosis, breast cancer, and uterine pathologies. It also aids in developing targeted therapies, such as selective progesterone receptor modulators (SPRMs), and diagnostic tools for hormone-responsive diseases. Additionally, its application in structural biology has advanced understanding of receptor-ligand dynamics and allosteric regulation.
Beyond therapeutics, recombinant PGR supports agricultural and veterinary studies by improving reproductive management in livestock. Its versatility underscores its importance in bridging basic science with clinical and industrial innovations, offering a robust tool to decode progesterone signaling and its translational potential.
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