| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GMPR2 |
| Uniprot No | Q9P2T1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-348aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMPHIDNDVKLDFKDVLLRPKRSTLKSRSEV DLTRSFSFRNSKQTYSGVPIIAANMDTVGTFEMAKVLCKFSLFTAVHKHY SLVQWQEFAGQNPDCLEHLAASSGTGSSDFEQLEQILEAIPQVKYICLDV ANGYSEHFVEFVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIKVGI GPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAK AFGAGADFVMLGGMLAGHSESGGELIERDGKKYKLFYGMSSEMAMKKYAG GVAEYRASEGKTVEVPFKGDVEHTIRDILGGIRSTCTYVGAAKLKELSRR TTFIRVTQQVNPIFSEAC |
| 预测分子量 | 40 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GMPR2重组蛋白的3篇参考文献的简要信息：
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1. **文献名称**：*Recombinant Expression and Functional Characterization of Human GMP Reductase 2*
**作者**：Li, X., et al.
**摘要**：该研究报道了人源GMPR2重组蛋白在大肠杆菌中的高效表达与纯化，验证了其酶活性及在嘌呤代谢中的功能，为后续药物靶点研究奠定基础。
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2. **文献名称**：*Structural Insights into GMPR2 Catalytic Mechanism by Cryo-EM Analysis*
**作者**：Zhang, Y., et al.
**摘要**：通过冷冻电镜解析GMPR2重组蛋白的三维结构，揭示了其底物结合位点与催化机制，为设计特异性抑制剂提供了结构基础。
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3. **文献名称**：*GMPR2 Deficiency and Recombinant Protein Rescue in Cellular Models*
**作者**：Wang, H., et al.
**摘要**：研究发现GMPR2缺失导致细胞嘌呤代谢紊乱，通过外源添加重组GMPR2蛋白可恢复代谢稳态，证实其在遗传性疾病治疗中的潜在价值。
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注：以上文献信息为示例性质，实际引用需以真实发表的论文为准。建议通过PubMed或Web of Science以关键词“GMPR2 recombinant”进一步检索最新研究。
GMPR2 (Guanosine Monophosphate Reductase 2) is a member of the GMP reductase family, which plays a critical role in purine metabolism by catalyzing the reductive deamination of guanosine monophosphate (GMP) to inosine monophosphate (IMP). This enzymatic step is essential for maintaining nucleotide balance, particularly in recycling guanine nucleotides and regulating intracellular purine pools. Unlike its isoform GMPR1. GMPR2 exhibits distinct tissue-specific expression patterns and regulatory mechanisms, though both enzymes share structural homology and conserved catalytic domains.
The recombinant GMPR2 protein is produced using genetic engineering techniques, typically expressed in bacterial, insect, or mammalian cell systems to ensure proper folding and post-translational modifications. Its production enables detailed biochemical and functional studies, including enzyme kinetics, substrate specificity, and interaction with potential inhibitors or activators. Researchers utilize recombinant GMPR2 to explore its role in cellular processes such as DNA/RNA synthesis, energy metabolism, and redox regulation. Dysregulation of GMPR2 has been implicated in metabolic disorders, immune dysfunction, and cancer progression, making it a potential therapeutic target.
Structural studies of recombinant GMPR2. facilitated by X-ray crystallography or cryo-EM, have provided insights into its catalytic mechanism and substrate-binding sites. These findings aid in designing small molecules to modulate its activity, with applications in treating diseases linked to purine metabolism imbalances. Additionally, recombinant GMPR2 serves as a tool for diagnostic assay development and high-throughput drug screening. Ongoing research focuses on clarifying its tissue-specific functions, regulatory networks, and therapeutic potential in precision medicine.
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