| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GSTp |
| 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GSTp(谷胱甘肽S-转移酶pi)重组蛋白的3篇代表性文献摘要整理(信息基于既有知识，建议通过数据库验证原文)：
---
1. **文献名称**：*"Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase"*
**作者**：Smith, D.B., Johnson, K.S.
**摘要**：该研究描述了利用谷胱甘肽S-转移酶(GST)标签的重组蛋白表达与纯化系统。通过pGEX载体在大肠杆菌中表达GST融合蛋白，并利用谷胱甘肽亲和层析一步纯化目标蛋白，为后续GSTp重组蛋白的应用提供了基础方法。
2. **文献名称**：*"Human glutathione transferases: functional and structural aspects of their polymorphism and variability"*
**作者**：Mannervik, B., Widersten, M.
**摘要**：综述了GST家族(包括GSTp亚型)的遗传多态性、酶学特性及其在药物代谢和解毒中的作用，强调了重组GSTp蛋白在酶动力学研究和毒性化合物代谢模型中的应用。
3. **文献名称**：*"The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance"*
**作者**：Hayes, J.D., Pulford, D.J.
**摘要**：探讨了GSTp在肿瘤中的过表达现象及其作为化疗耐药生物标志物的潜力，并利用重组GSTp蛋白验证了其通过结合化疗药物(如顺铂)降低药物活性的分子机制。
---
**注**：如需具体文献，建议通过PubMed或Google Scholar检索关键词“GSTp recombinant protein”“GST fusion purification”等获取最新或更匹配的研究。
**Background of GSTp Recombinant Protein**
Glutathione S-transferase pi (GSTp), encoded by the *GSTP1* gene in humans, belongs to a family of phase II detoxification enzymes that catalyze the conjugation of glutathione (GSH) to electrophilic substrates. This critical function aids in neutralizing reactive oxygen species (ROS), environmental toxins, chemotherapeutic agents, and endogenous byproducts, facilitating their excretion. GSTp is predominantly expressed in epithelial tissues and plays a role in cellular defense against oxidative stress and xenobiotic toxicity.
Structurally, GSTp exists as a homodimer, with each subunit (~23 kDa) containing a conserved GSH-binding site (G-site) and a hydrophobic substrate-binding domain (H-site). Its enzymatic activity relies on stabilizing the thiol group of GSH, enhancing its nucleophilicity for conjugation reactions. Beyond detoxification, GSTp regulates cellular signaling pathways by modulating protein-protein interactions. For instance, it inhibits c-Jun N-terminal kinase (JNK) by binding to its N-terminal domain, influencing apoptosis and proliferation.
Recombinant GSTp is produced via heterologous expression systems (e.g., *E. coli* or mammalian cells*) for research and industrial applications. Its high solubility and affinity for glutathione matrices make it a popular fusion tag for protein purification. The GST-tag system allows efficient isolation of target proteins using glutathione-coated resins. Additionally, recombinant GSTp serves as a tool to study drug metabolism, oxidative stress mechanisms, and cancer biology. Overexpression of GSTp in tumors is linked to chemoresistance, as it inactivates cytotoxic drugs via conjugation. This has spurred interest in developing GSTp inhibitors to sensitize cancer cells to treatment.
In summary, GSTp recombinant protein bridges fundamental research on cellular detoxification and disease mechanisms with practical applications in biotechnology and therapeutic development.
×
