| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GRHPR |
| Uniprot No | Q9UBQ7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-328aa |
| 氨基酸序列 | MRPVRLMKVFVTRRIPAEGRVALARAADCEVEQWDSDEPIPAKELERGVAGAHGLLCLLSDHVDKRILDAAGANLKVISTMSVGIDHLALDEIKKRGIRVGYTPDVLTDTTAELAVSLLLTTCRRLPEAIEEVKNGGWTSWKPLWLCGYGLTQSTVGIIGLGRIGQAIARRLKPFGVQRFLYTGRQPRPEEAAEFQAEFVSTPELAAQSDFIVVACSLTPATEGLCNKDFFQKMKETAVFINISRGDVVNQDDLYQALASGKIAAAGLDVTSPEPLPTNHPLLTLKNCVILPHIGSATHRTRNTMSLLAANNLLAGLRGEPMPSELKL |
| 分子量 | 61.82 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 0 |
| 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. |
以下是关于重组人GRHPR蛋白的3篇典型文献示例(虚构内容，仅供参考)：
1. **文献名称**：*Expression, Purification, and Functional Analysis of Recombinant Human GRHPR in E. coli*
**作者**：Smith A, et al.
**摘要**：该研究通过构建人源GRHPR基因的重组质粒，在大肠杆菌中高效表达可溶性蛋白，经亲和层析纯化后验证其催化乙醛酸和羟基丙酮酸还原的酶活性，揭示其底物特异性及动力学参数。
2. **文献名称**：*Structural Insights into the Role of GRHPR Mutations in Primary Hyperoxaluria Type 2*
**作者**：Lee J, Patel R.
**摘要**：通过X射线晶体学解析重组人GRHPR的三维结构，结合突变体功能实验，发现某些致病突变会导致酶活性中心构象改变，进而降低催化效率，为2型原发性高草酸尿症提供分子机制解释。
3. **文献名称**：*Development of a Cell-Based Assay for Screening GRHPR Enhancers Using Recombinant Protein*
**作者**：Chen L, et al.
**摘要**：利用重组人GRHPR蛋白构建细胞模型，开发高通量筛选体系，用于发现能增强酶活性或稳定性的化合物，为潜在药物治疗代谢疾病提供新策略。
(注：以上文献为虚构示例，实际研究需检索PubMed、Web of Science等数据库获取真实文献。)
Human glyoxylate reductase/hydroxypyruvate reductase (GRHPR) is a ubiquitously expressed enzyme predominantly localized in the liver and kidneys, where it plays critical roles in glyoxylate metabolism and photorespiration. This dual-function enzyme catalyzes two distinct reactions: the NADPH-dependent reduction of glyoxylate to glycolate (preventing oxalate overproduction) and hydroxypyruvate to D-glycerate (linking glycolysis with serine biosynthesis). GRHPR dysfunction is directly associated with primary hyperoxaluria type 2 (PH2), a rare autosomal recessive disorder characterized by excessive hepatic oxalate synthesis, leading to nephrolithiasis, nephrocalcinosis, and systemic oxalosis.
The 34-kDa GRHPR protein functions as a homodimer with conserved catalytic residues across species. Its crystal structure reveals a classic (β/α)8 TIM barrel fold, common to the Hsp20/alpha crystallin superfamily. Recombinant human GRHPR is typically produced in prokaryotic (E. coli) or eukaryotic expression systems for functional studies and therapeutic exploration. Current research focuses on elucidating its substrate specificity mechanisms, PH2-associated mutation impacts (e.g., c.103delG), and potential applications in enzyme replacement therapy. Emerging studies also investigate GRHPR's metabolic crosstalk with other pathways and its role beyond oxalate regulation, including possible involvement in cancer cell metabolism.
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