| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GATM |
| Uniprot No | P50440 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 38-423aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMSTQAATASSRNSCAADDKATEPLPKD CPVSSYNEWDPLEEVIVGRAENACVPPFTIEVKANTYEKYWPFYQKQGGH YFPKDHLKKAVAEIEEMCNILKTEGVTVRRPDPIDWSLKYKTPDFESTGL YSAMPRDILIVVGNEIIEAPMAWRSRFFEYRAYRSIIKDYFHRGAKWTTA PKPTMADELYNQDYPIHSVEDRHKLAAQGKFVTTEFEPCFDAADFIRAGR DIFAQRSQVTNYLGIEWMRRHLAPDYRVHIISFKDPNPMHIDATFNIIGP GIVLSNPDRPCHQIDLFKKAGWTIITPPTPIIPDDHPLWMSSKWLSMNVL MLDEKRVMVDANEVPIQKMFEKLGITTIKVNIRNANSLGGGFHCWTCDVR RRGTLQSYLD |
| 预测分子量 | 47 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GATM重组蛋白的3篇参考文献的简要概括(注：文献信息为模拟内容，非真实存在)：
1. **《Expression and purification of recombinant human GATM in Escherichia coli》**
- **作者**: Zhang L, et al.
- **摘要**: 本研究成功构建了人源GATM基因的原核表达系统，通过优化诱导条件和纯化步骤，获得了高纯度重组蛋白。该蛋白在体外表现出甘氨酸脒基转移酶活性，为后续酶学研究和抑制剂开发提供了基础工具。
2. **《Structural insights into the catalytic mechanism of GATM through X-ray crystallography》**
- **作者**: Kim S, et al.
- **摘要**: 利用重组GATM蛋白的晶体结构解析，揭示了其底物结合位点及催化关键氨基酸残基。研究阐明了GATM在肌酸生物合成中的构象变化机制，为遗传性代谢疾病(如GATM缺陷症)的治疗策略提供了理论依据。
3. **《Functional characterization of GATM mutations associated with tubular aggregate myopathy》**
- **作者**: Rossi D, et al.
- **摘要**: 通过体外表达携带致病突变的GATM重组蛋白，发现特定突变导致酶活性显著降低和蛋白稳定性下降。该研究揭示了GATM功能异常与肌肉病理表型之间的关联，支持了其在细胞能量代谢中的关键作用。
如需真实文献，建议通过PubMed或Web of Science以“GATM recombinant protein”“glycine amidinotransferase expression”等关键词检索。
**Background of GATM Recombinant Protein**
GATM (Glycine AmidinoTransferase), also known as L-arginine:glycine amidinotransferase, is a mitochondrial enzyme critical for creatine biosynthesis. It catalyzes the first and rate-limiting step in creatine production by transferring the amidino group from L-arginine to glycine, forming guanidinoacetate and ornithine. Creatine, essential for cellular energy homeostasis, is particularly vital in tissues with high energy demands, such as skeletal muscle, brain, and heart.
Recombinant GATM protein is engineered through genetic cloning and expression in heterologous systems (e.g., *E. coli* or mammalian cell lines) to produce purified, functional enzyme for research and therapeutic applications. Its recombinant form retains enzymatic activity and structural integrity, enabling studies on creatine metabolism, enzyme kinetics, and molecular interactions.
GATM dysfunction is linked to metabolic disorders, including guanidinoacetate methyltransferase (GAMT) deficiency and primary creatine deficiency syndromes, which cause neurological impairments and muscle weakness. Recombinant GATM is used to investigate these pathologies, screen potential therapeutics, and develop diagnostic tools. Additionally, it serves as a tool to study mitochondrial biology, amino acid metabolism, and energy regulation pathways.
In drug discovery, GATM recombinant protein aids in identifying inhibitors or modulators for conditions like cancer or cardiovascular diseases, where altered creatine metabolism may play a role. Its structure-function relationships, including mutations affecting enzyme activity, are also explored to understand genetic variants’ clinical significance.
Overall, GATM recombinant protein is a pivotal resource for advancing research into metabolic diseases, neuromuscular health, and therapeutic innovation.
×
