| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GART |
| Uniprot No | P22102 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 111–318aa |
| 氨基酸序列 | KEFMDRHGIPTAQWKAFTKPEEACSFILSADFPALVVKASGLAAGKGVIVAKSKEEACKAVQEIMQEKAFGAAGETIVIEELLDGEEVSCLCFTDGKTVAPMPPAQDHKRLLEGDGGPNTGGMGAYCPAPQVSNDLLLKIKDTVLQRTVDGMQQEGTPYTGILYAGIMLTKNGPKVLEFNCRFGDPECQVILPLLKSDLYEVIQSTLD |
| 预测分子量 | 26.5 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GART重组蛋白的参考文献示例(内容为概括性描述，非真实文献)：
1. **《Recombinant Expression and Functional Analysis of Human GART Enzyme》**
- 作者：Smith J, et al.
- 摘要：研究通过大肠杆菌表达系统成功克隆并纯化人源GART重组蛋白，验证其催化甘氨酰胺核苷酸合成的酶活性，为嘌呤代谢研究提供工具。
2. **《Crystal Structure of GART Recombinant Protein Reveals Substrate Binding Sites》**
- 作者：Chen L, et al.
- 摘要：利用重组GART蛋白进行X射线晶体学分析，解析其三维结构，揭示底物结合域及潜在抑制剂靶点，助力药物开发。
3. **《Role of Recombinant GART in Drosophila Development: Genetic and Biochemical Insights》**
- 作者：Wang Y, et al.
- 摘要：在果蝇模型中表达重组GART蛋白，证明其通过调控嘌呤合成影响胚胎发育，为遗传性疾病机制提供依据。
4. **《Optimization of GART Recombinant Production in Mammalian Cell Lines》**
- 作者：Kim S, et al.
- 摘要：对比哺乳动物细胞(如HEK293)中重组GART的表达条件，优化纯化工艺以提高蛋白产量和稳定性，支持功能研究。
(注：以上为示例性内容，如需真实文献，建议通过PubMed、Web of Science等学术平台检索关键词“GART recombinant protein”或“GART expression and purification”。)
**Background of GART Recombinant Protein**
GART (Glycinamide Ribonucleotide Transformylase), also known as PURT or FGARAT, is a key enzyme in the *de novo* purine biosynthesis pathway, catalyzing the conversion of glycinamide ribonucleotide (GAR) to formylglycinamide ribonucleotide (FGAR). This step is critical for generating purine nucleotides, essential building blocks for DNA/RNA synthesis and cellular energy transfer (e.g., ATP/GTP). GART is part of a trifunctional enzyme complex (GART, AIRS, and GAR synthetase) in eukaryotes, though recombinant forms are often expressed as single-domain proteins for research.
Recombinant GART proteins are engineered using expression systems like *E. coli* or yeast, enabling high-purity production for structural and functional studies. These proteins retain enzymatic activity, making them valuable tools for studying purine metabolism dysregulation linked to diseases such as cancer, immunodeficiency disorders, and viral replication (e.g., viruses relying on host purine synthesis).
GART’s role in cell proliferation has positioned it as a potential therapeutic target. Inhibitors targeting GART could disrupt nucleotide synthesis in rapidly dividing cells, offering strategies for anticancer or antiviral therapies. Structural studies using recombinant GART have revealed insights into its catalytic mechanism and substrate-binding sites, aiding drug design.
Additionally, recombinant GART is used in diagnostic assays to detect enzyme activity abnormalities or autoimmune antibodies in conditions like lupus. Its application extends to biotechnology, where engineered variants optimize nucleotide biosynthesis in microbial systems for industrial metabolite production.
Overall, GART recombinant proteins bridge fundamental biochemistry with translational research, advancing both understanding of purine metabolism and development of targeted therapies.
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