| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GLYAT |
| Uniprot No | Q6IB77 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-296aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMMLPLQGAQMLQMLEKSLRKSLPASLKVYG TVFHINHGNPFNLKAVVDKWPDFNTVVVCPQEQDMTDDLDHYTNTYQIYS KDPQNCQEFLGSPELINWKQHLQIQSSQPSLNEAIQNLAAIKSFKVKQTQ RILYMAAETAKELTPFLLKSKILSPSGGKPKAINQEMFKLSSMDVTHAHL VNKFWHFGGNERSQRFIERCIQTFPTCCLLGPEGTPVCWDLMDQTGEMRM AGTLPEYRLHGLVTYVIYSHAQKLGKLGFPVYSHVDYSNEAMQKMSYTLQ HVPIPRSWNQWNCVPL |
| 预测分子量 | 36 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. |
1. **《Functional characterization of recombinant human glycine N-acyltransferase》**
- 作者：Zhang, Y. et al.
- 摘要：研究通过大肠杆菌系统表达并纯化重组人源GLYAT蛋白，分析其酶动力学特性及对酰基辅酶A底物的选择性，揭示其在解毒代谢中的潜在作用。
2. **《Structural insights into the catalytic mechanism of GLYAT through recombinant protein crystallography》**
- 作者：Smith, J. & Lee, K.
- 摘要：利用重组GLYAT蛋白的晶体结构解析，阐明其催化活性中心的构象变化及底物结合机制，为设计代谢疾病相关药物提供结构基础。
3. **《Optimization of recombinant GLYAT expression in Pichia pastoris for high-yield production》**
- 作者：Wang, H. et al.
- 摘要：通过在毕赤酵母中优化密码子和发酵条件，实现重组GLYAT的高效表达与活性维持，推动其在工业级酶催化中的应用。
4. **《Role of recombinant GLYAT variants in xenobiotic metabolism: A comparative study》**
- 作者：Chen, L. & Gupta, R.
- 摘要：比较不同物种来源的重组GLYAT变体对多种外源化合物的代谢活性，发现人类GLYAT对特定药物代谢具有独特效率，提示个体化医疗价值。
(注：上述文献信息为示例性内容，实际文献需通过数据库如PubMed或Google Scholar检索确认。)
**Background of GLYAT Recombinant Protein**
The glycine-N-acyltransferase (GLYAT) enzyme, encoded by the *GLYAT* gene, plays a critical role in detoxification pathways, primarily in the liver. It catalyzes the conjugation of glycine with acyl-CoA derivatives, facilitating the elimination of xenobiotics and endogenous metabolites, such as benzoic acid and branched-chain fatty acids. This process is vital for maintaining metabolic homeostasis and mitigating toxicity. Genetic variations in *GLYAT* have been linked to differences in detoxification capacity among individuals, influencing susceptibility to metabolic disorders and drug-induced toxicity.
Recombinant GLYAT protein is engineered through heterologous expression systems, such as *E. coli* or mammalian cell cultures, enabling large-scale production of the purified enzyme for functional and structural studies. Its recombinant form retains catalytic activity, allowing researchers to investigate enzyme kinetics, substrate specificity, and the impact of mutations or polymorphisms on function. These studies are pivotal for understanding molecular mechanisms underlying GLYAT-associated metabolic processes and its potential role in diseases like hyperammonemia or neurodegenerative conditions linked to toxin accumulation.
Additionally, recombinant GLYAT serves as a tool in drug discovery, particularly in screening compounds that modulate its activity to enhance detoxification pathways. Its application extends to personalized medicine, where *in vitro* assays using the recombinant protein help predict individual responses to drugs or environmental toxins based on genetic profiles. Evolutionary studies also utilize recombinant GLYAT to explore sequence conservation and functional divergence across species, shedding light on adaptive metabolic strategies.
Overall, GLYAT recombinant protein bridges biochemical research and clinical applications, offering insights into detoxification biology and therapeutic development.
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