| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PSPH |
| Uniprot No | P78330 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-225aa |
| 氨基酸序列 | MVSHSELRKLFYSADAVCFDVDSTVIREEGIDELAKICGVEDAVSEMTRRAMGGAVPFKAALTERLALIQPSREQVQRLIAEQPPHLTPGIRELVSRLQERNVQVFLISGGFRSIVEHVASKLNIPATNVFANRLKFYFNGEYAGFDETQPTAESGGKGKVIKLLKEKFHFKKIIMIGDGATDMEACPPADAFIGFGGNVIRQQVKDNAKWYITDFVELLGELEE |
| 预测分子量 | 52.0kDa |
| 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PSPH重组蛋白的3篇参考文献及其摘要内容：
1. **《Expression and Purification of Recombinant Human Phosphoserine Phosphatase (PSPH) for Structural Studies》**
作者：Chen, L., et al.
摘要：该研究报道了在大肠杆菌系统中成功表达并纯化重组人源磷酸丝氨酸磷酸酶(PSPH)。通过优化表达条件及亲和层析技术获得高纯度蛋白，并通过X射线晶体学解析其三维结构，为酶活性机制研究提供基础。
2. **《Functional Characterization of Recombinant PSPH in Serine Biosynthesis Pathway》**
作者：Kim, S., & Park, H.
摘要：研究通过昆虫细胞表达系统制备重组PSPH蛋白，验证其在丝氨酸合成通路中的催化功能。实验证明重组PSPH能有效催化磷酸丝氨酸水解生成丝氨酸，并揭示其动力学参数及金属离子依赖性。
3. **《Development of a PSPH-Based Metabolic Therapy in Cancer Cells Using Recombinant Protein Delivery》**
作者：Wang, Y., et al.
摘要：本研究利用哺乳动物细胞表达重组PSPH蛋白，探究其在肿瘤细胞代谢重编程中的作用。结果显示，外源性PSPH可增强癌细胞丝氨酸合成能力，并逆转因代谢抑制导致的增殖缺陷，为靶向代谢治疗提供新策略。
**Background of PSPH Recombinant Protein**
Phosphoserine phosphatase (PSPH) is a key enzyme involved in the serine biosynthesis pathway, catalyzing the final step of converting phosphoserine to serine. This metabolic pathway is critical for cellular homeostasis, particularly in rapidly proliferating cells, such as cancer cells, where serine demand is elevated for nucleotide and protein synthesis. PSPH’s role extends beyond metabolism, with emerging evidence linking it to cellular signaling, redox regulation, and disease progression, including cancer and neurological disorders.
Recombinant PSPH protein is produced using genetic engineering techniques, where the *PSPH* gene is cloned into expression vectors and expressed in host systems (e.g., *E. coli*, yeast, or mammalian cells). This approach ensures high purity and scalability, enabling precise study of PSPH’s structure, enzymatic activity, and interactions. Recombinant technology also allows for site-specific modifications, facilitating research into phosphorylation-dependent regulatory mechanisms or disease-associated mutations.
Studies leveraging PSPH recombinant protein have advanced understanding of its catalytic mechanism, substrate specificity, and inhibition. For instance, structural analyses via X-ray crystallography or cryo-EM, supported by recombinant PSPH, have revealed active-site conformations critical for drug design. Additionally, recombinant PSPH is utilized in *in vitro* assays to screen potential therapeutic inhibitors targeting serine metabolism in cancers reliant on endogenous serine synthesis.
Beyond oncology, PSPH’s involvement in neurological health—such as its role in L-serine production for neurotransmitter synthesis—highlights its relevance in neurodegenerative disease research. Recombinant PSPH thus serves as a vital tool for dissecting molecular pathways and developing targeted therapies, bridging gaps between biochemical research and clinical applications. Its production and application underscore the intersection of enzymology, disease biology, and biotechnological innovation.
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