| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GLYATL2 |
| Uniprot No | Q8WU03 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-294aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMLVLHNSQKLQILYKSLEKSIPESIKV YGAIFNIKDKNPFNMEVLVDAWPDYQIVITRPQKQEMKDDQDHYTNTYHI FTKAPDKLEEVLSYSNVISWEQTLQIQGCQEGLDEAIRKVATSKSVQVDY MKTILFIPELPKKHKTSSNDKMELFEVDDDNKEGNFSNMFLDASHAGLVN EHWAFGKNERSLKYIERCLQDFLGFGVLGPEGQLVSWIVMEQSCELRMGY TVPKYRHQGNMLQIGYHLEKYLSQKEIPFYFHVADNNEKSLQALNNLGFK ICPCGWHQWKCTPKKYC |
| 预测分子量 | 37 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GLYATL2重组蛋白的3篇代表性文献摘要：
1. **文献名称**: "Functional characterization of human GLYATL2 in amino acid conjugation reactions"
**作者**: Smith A, et al.
**摘要**: 研究首次在大肠杆菌中重组表达了GLYATL2蛋白，证实其具有甘氨酸结合酶活性，可催化多种酰基辅酶A底物与甘氨酸的结合反应，提示其在异源物质代谢中的潜在作用。
2. **文献名称**: "Recombinant expression and substrate specificity analysis of GLYATL2 in liver metabolism"
**作者**: Chen L, Wang H.
**摘要**: 通过哺乳动物细胞表达系统获得重组GLYATL2蛋白，发现其对中长链脂肪酸具有显著结合活性，并揭示其与肝脏解毒代谢途径中其他GLYAT家族酶的功能差异。
3. **文献名称**: "Structural insights into GLYATL2-mediated glycine conjugation"
**作者**: Gupta R, et al.
**摘要**: 利用重组表达的GLYATL2蛋白进行X射线晶体结构解析，揭示了其活性位点关键氨基酸残基，并通过突变实验验证了特定结构域对底物选择性的调控机制。
注：以上文献信息为模拟示例，实际研究需通过学术数据库检索具体文献。若需真实文献，建议在PubMed等平台以"GLYATL2 recombinant"为关键词查询。
**Background of GLYATL2 Recombinant Protein**
GLYATL2 (Glycine-N-acyltransferase-like 2) is a member of the glycine N-acyltransferase (GLYAT) enzyme family, which plays a role in detoxification metabolism by conjugating glycine to acyl-CoA substrates. This process facilitates the elimination of xenobiotics or endogenous metabolites, particularly in the liver. GLYATL2 shares structural and functional similarities with other GLYAT family members but exhibits distinct substrate preferences, such as a higher affinity for benzoyl-CoA, a byproduct of mitochondrial fatty acid β-oxidation.
The recombinant GLYATL2 protein is engineered in vitro using expression systems like *E. coli* or mammalian cells, enabling large-scale production for functional studies. Its recombinant form retains enzymatic activity, making it valuable for investigating metabolic pathways, enzyme kinetics, and interactions with cofactors or inhibitors. Research suggests GLYATL2 may contribute to lipid metabolism regulation and cellular detoxification, with potential implications in metabolic disorders, liver diseases, and drug-induced toxicity.
Recent studies highlight its differential expression in certain cancers, suggesting a role in tumor metabolism or as a biomarker. However, its precise physiological and pathological roles remain under exploration. The availability of recombinant GLYATL2 aids in elucidating its mechanism, substrate specificity, and therapeutic potential. Standardized purification techniques, such as affinity chromatography with His-tags, ensure high purity and reproducibility, supporting both basic research and drug development efforts. Overall, GLYATL2 recombinant protein serves as a critical tool for advancing understanding of acyltransferase biology and metabolic disease mechanisms.
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