| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GSTP1 |
| Uniprot No | P09211 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-210aa |
| 氨基酸序列 | PPYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQEGSLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLYGKDQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYVKALPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLLIHEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYVNLPINGNGKQ |
| 预测分子量 | 25.2 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GSTP1重组蛋白的3篇模拟参考文献及摘要概括(注：文献信息为虚构示例，仅供格式参考)：
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1. **文献名称**: *"Expression and Purification of Recombinant GSTP1 for Functional Studies"*
**作者**: Smith A. et al. (2015)
**摘要**: 该研究报道了在大肠杆菌系统中高效表达并纯化GSTP1重组蛋白的方法，通过优化诱导条件和亲和层析技术获得高纯度蛋白，用于后续酶活性和药物结合实验。
2. **文献名称**: *"Structural Insights into GSTP1-Catalyzed Detoxification Using Recombinant Protein Crystallography"*
**作者**: Brown C. et al. (2020)
**摘要**: 作者利用重组GSTP1蛋白进行X射线晶体学分析，解析其三维结构，揭示了底物结合口袋的关键氨基酸残基，为设计靶向GSTP1的抑制剂提供了结构基础。
3. **文献名称**: *"Recombinant GSTP1 Attenuates Oxidative Stress in Cellular Models"*
**作者**: Lee J. et al. (2017)
**摘要**: 通过体外实验证明，外源性重组GSTP1蛋白可显著降低过氧化氢诱导的细胞氧化损伤，表明其在抗氧化治疗中的潜在应用价值。
4. **文献名称**: *"Role of Recombinant GSTP1 in Chemotherapy Resistance Mechanisms"*
**作者**: Wang Y. et al. (2019)
**摘要**: 研究发现，重组GSTP1蛋白可通过与化疗药物(如顺铂)结合并促进其代谢，降低药物毒性，解释了肿瘤细胞中GSTP1高表达导致耐药性的分子机制。
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(注：以上文献信息为示例，实际引用需检索PubMed等数据库获取真实文献。)
**Background of GSTP1 Recombinant Protein**
Glutathione S-transferase P1 (GSTP1) is a member of the glutathione S-transferase (GST) family, a group of phase II detoxification enzymes that catalyze the conjugation of reduced glutathione (GSH) to electrophilic substrates. This process neutralizes reactive oxygen species (ROS), xenobiotics, and carcinogens, protecting cells from oxidative stress and chemical damage. GSTP1 is primarily expressed in epithelial cells of organs such as the placenta, lung, and brain, and is notably overexpressed in various cancers, including prostate, ovarian, and non-small cell lung carcinomas. Its upregulation is often linked to chemotherapeutic drug resistance, making it a biomarker for cancer prognosis and a potential therapeutic target.
The recombinant GSTP1 protein is engineered using prokaryotic or eukaryotic expression systems (e.g., *E. coli* or mammalian cells) to produce a purified, functionally active form. It typically retains the enzymatic properties of native GSTP1. including substrate-binding specificity and catalytic activity. Recombinant GSTP1 is widely used in *in vitro* studies to investigate detoxification mechanisms, drug metabolism, and cancer biology. Its role in modulating cellular responses to oxidative stress and apoptosis has also made it a focus in neurodegenerative disease research, such as Alzheimer’s and Parkinson’s.
Structurally, GSTP1 functions as a homodimer, with each subunit containing a conserved GSH-binding site and a hydrophobic substrate-binding domain. Researchers utilize recombinant GSTP1 to study enzyme kinetics, protein-protein interactions, and inhibitor screening for drug development. Additionally, its fusion with other proteins (e.g., GST-tag systems) facilitates protein purification and solubility studies. Understanding GSTP1’s molecular mechanisms continues to advance insights into disease pathways and therapeutic strategies.
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