| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GMPR |
| Uniprot No | P36959 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-345aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MPRIDADLKL DFKDVLLRPK RSSLKSRAEV DLERTFTFRN SKQTYSGIPI IVANMDTVGT FEMAAVMSQH SMFTAIHKHY SLDDWKLFAT NHPECLQNVA VSSGSGQNDL EKMTSILEAV PQVKFICLDV ANGYSEHFVE FVKLVRAKFP EHTIMAGNVV TGEMVEELIL SGADIIKVGV GPGSVCTTRT KTGVGYPQLS AVIECADSAH GLKGHIISDG GCTCPGDVAK AFGAGADFVM LGGMFSGHTE CAGEVIERNG RKLKLFYGMS SDTAMNKHAG GVAEYRASEG KTVEVPYKGD VENTILDILG GLRSTCTYVG AAKLKELSRR ATFIRVTQQH NTVFS |
| 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GMPR(GMP还原酶)重组蛋白的3篇代表性文献的简要信息(注：文献为示例，非真实存在)：
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1. **文献名称**：*Expression and Purification of Recombinant GMP Reductase in Escherichia coli*
**作者**：Smith, J.R. et al.
**摘要**：本研究报道了在大肠杆菌BL21(DE3)中高效表达GMPR重组蛋白的优化方法，采用His标签亲和层析纯化，获得高纯度蛋白。酶活测定显示重组GMPR具有与天然酶相似的催化活性，为后续代谢通路研究提供工具。
2. **文献名称**：*Structural Insights into Human GMP Reductase via Recombinant Protein Crystallography*
**作者**：Chen, L. et al.
**摘要**：通过哺乳动物细胞表达系统(HEK293)获得人源GMPR重组蛋白，解析其2.8Å分辨率晶体结构。研究发现其底物结合域的关键氨基酸残基，揭示了GMPR在嘌呤代谢中的变构调控机制。
3. **文献名称**：*Functional Characterization of Recombinant GMPR in a Zebrafish Metabolic Disorder Model*
**作者**：Wang, Y. et al.
**摘要**：利用昆虫杆状病毒系统表达GMPR重组蛋白，并验证其体外酶动力学参数。进一步在斑马鱼模型中证明GMPR缺失导致尿酸代谢异常，重组蛋白回补可部分恢复表型，提示其在代谢疾病中的潜在治疗价值。
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如需真实文献，建议通过PubMed或Web of Science搜索关键词“GMP reductase recombinant protein”获取近年研究。
GMPR (Guanosine Monophosphate Reductase) is a critical enzyme in purine nucleotide metabolism, catalyzing the conversion of guanosine monophosphate (GMP) to inosine monophosphate (IMP). This reaction is essential for maintaining the balance of intracellular purine nucleotide pools and plays a regulatory role in cellular energy metabolism and nucleic acid synthesis. GMPR exists in two isoforms in mammals: GMPR1 (cytoplasmic) and GMPR2 (mitochondrial), with distinct tissue-specific expression patterns. Dysregulation of GMPR activity has been linked to metabolic disorders, immune dysfunction, and cancer progression.
Recombinant GMPR protein refers to the enzyme produced through genetic engineering techniques, typically by expressing the GMPR gene in heterologous systems such as *E. coli*, yeast, or mammalian cell lines. This approach enables large-scale production of highly pure, functional protein for research and therapeutic applications. The recombinant form preserves the enzyme's catalytic properties while allowing modifications like affinity tags (e.g., His-tag) for simplified purification. Recent studies have highlighted its potential as a biomarker in metabolic diseases and as a therapeutic target, particularly in cancers where purine metabolism is altered. Structural characterization of recombinant GMPR using crystallography and cryo-EM has advanced understanding of its substrate-binding mechanisms and allosteric regulation, facilitating drug discovery efforts. Additionally, it serves as a valuable tool for screening enzyme inhibitors and studying nucleotide metabolism pathways *in vitro*. The development of recombinant GMPR has significantly enhanced biochemical research capabilities and holds promise for diagnostic and therapeutic innovations.
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