| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GLYATL1 |
| Uniprot No | Q969I3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-302aa |
| 氨基酸序列 | MILLNNSHKLLALYKSLARSIPESLKVYGSVYHINHGNPFNMEVLVDSWPEYQMVIIRPQKQEMTDDMDSYTNVYRMFSKEPQKSEEVLKNCEIVNWKQRLQIQGLQESLGEGIRVATFSKSVKVEHSRALLLVTEDILKLNASSKSKLGSWAETGHPDDEFESETPNFKYAQLDVSYSGLVNDNWKRGKNERSLHYIKRCIEDLPAACMLGPEGVPVSWVTMDPSCEVGMAYSMEKYRRTGNMARVMVRYMKYLRQKNIPFYISVLEENEDSRRFVGQFGFFEASCEWHQWTCYPQNLVPF |
| 预测分子量 | 62.1 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3篇关于GLYATL1重组蛋白的假设性参考文献示例(注：GLYATL1研究较少，以下内容为基于相关领域文献结构的模拟示例)：
1. **标题**: "Recombinant GLYATL1 protein expression and its role in glycine conjugation"
**作者**: Smith J, et al.
**摘要**: 本研究在大肠杆菌中成功表达并纯化了重组人GLYATL1蛋白，证实其具有甘氨酸酰基转移酶活性，能够催化苯甲酸与甘氨酸的结合反应，提示其在肝脏解毒代谢中的潜在功能。
2. **标题**: "Structural characterization of human GLYATL1 by X-ray crystallography"
**作者**: Li X, Wang Y.
**摘要**: 通过重组蛋白技术获得高纯度GLYATL1蛋白，首次解析其晶体结构(分辨率2.1Å)，揭示其底物结合域的独特构象，为理解该酶催化机制提供结构基础。
3. **标题**: "GLYATL1 recombinant protein inhibits hepatocellular carcinoma cell proliferation in vitro"
**作者**: Chen H, et al.
**摘要**: 体外实验显示重组GLYATL1蛋白可通过调控PPARγ信号通路显著抑制肝癌细胞生长，提示其可能作为新型肿瘤抑制因子应用于癌症治疗研究。
注：真实文献检索建议通过PubMed(https://pubmed.ncbi.nlm.nih.gov)使用关键词 "GLYATL1 recombinant" 获取最新研究。该基因相关研究目前较少，现有文献多聚焦于基因表达分析而非重组蛋白功能研究。
**Background of GLYATL1 Recombinant Protein**
GLYATL1 (Glycine-N-acyltransferase-like 1) is a member of the glycine N-acyltransferase (GLYAT) family, which plays a role in detoxification metabolism by conjugating glycine to acyl-CoA substrates, facilitating the excretion of xenobiotics or endogenous metabolites. This enzyme is primarily expressed in the liver and kidneys, reflecting its importance in systemic detoxification pathways. GLYATL1 shares structural homology with other GLYAT isoforms but exhibits distinct substrate preferences and tissue-specific expression patterns, suggesting specialized biological roles.
Recombinant GLYATL1 protein is produced using biotechnological platforms, such as *E. coli* or mammalian expression systems, to enable functional and structural studies. Its production often involves cloning the *GLYATL1* gene into expression vectors, followed by purification via affinity chromatography. The recombinant protein retains enzymatic activity, allowing researchers to investigate its catalytic mechanisms, substrate specificity (e.g., preference for medium-chain acyl-CoA derivatives), and interactions with cofactors.
Studies on GLYATL1 have focused on its potential involvement in metabolic disorders, drug metabolism, and cellular stress responses. For instance, it may influence lipid metabolism by modulating acyl-CoA levels, linking it to obesity or fatty liver disease. Additionally, GLYATL1’s role in detoxifying reactive metabolites has implications for chemotherapeutic drug efficacy and toxicity. Emerging evidence also suggests tissue-specific regulation under pathological conditions, such as oxidative stress or inflammation.
The availability of recombinant GLYATL1 protein has accelerated *in vitro* assays, structural biology (e.g., crystallography), and biomarker discovery. However, its physiological significance remains partially unexplored, necessitating further research to clarify its contributions to human health and disease. Understanding GLYATL1 could advance therapeutic strategies targeting metabolic dysfunction or chemical toxicity.
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