| 纯度 | > 90 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | ACY3 |
| Uniprot No | Q96HD9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-319aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMCSLPVPREPLRRVAVTGGTHGNEMSG VYLARHWLHAPAELQRASFSAVPVLANPAATSGCRRYVDHDLNRTFTSSF LNSRPTPDDPYEVTRARELNQLLGPKASGQAFDFVLDLHNTTANMGTCLI AKSSHEVFAMHLCRHLQLQYPELSCQVFLYQRSGEESYNLDSVAKNGLGL ELGPQPQGVLRADIFSRMRTLVATVLDFIELFNQGTAFPAFEMEAYRPVG VVDFPRTEAGHLAGTVHPQLQDRDFQPLQPGAPIFQMFSGEDLLYEGEST VYPVFINEAAYYEKGVAFVQTEKFTFTVPAMPALTPAPSPAS |
| 预测分子量 | 38 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ACY3重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**: "Expression, purification and characterization of recombinant human aspartoacylase III"
**作者**: Wang Y, et al.
**摘要**: 研究报道了在大肠杆菌中高效表达人源ACY3重组蛋白，通过亲和层析纯化获得高纯度酶，并测定其催化天冬氨酸水解的酶动力学参数，证实其底物特异性。
2. **文献名称**: "Crystal structure of recombinant mouse acyltransferase 3 reveals substrate binding mechanism"
**作者**: Suzuki K, et al.
**摘要**: 利用杆状病毒-昆虫细胞系统表达小鼠ACY3重组蛋白，获得晶体结构解析，揭示了其活性位点与酰基辅酶A结合的分子机制，为酶功能研究提供结构基础。
3. **文献名称**: "Functional analysis of ACY3 mutations in metabolic disorders using recombinant enzyme assays"
**作者**: Zhang L, et al.
**摘要**: 构建了多种ACY3突变体重组蛋白，通过体外酶活实验发现特定突变导致催化活性丧失，解释了相关代谢疾病的分子病理机制。
注：以上文献信息为示例性质，实际研究中建议通过PubMed或Web of Science以关键词"ACY3 recombinant"检索最新文献。
**Background of ACY3 Recombinant Protein**
ACY3 (Aminoacylase-3) is a zinc-dependent hydrolase encoded by the *ACY3* gene, primarily involved in the metabolism of N-acetylated amino acids. It catalyzes the hydrolysis of N-acetylated substrates, such as N-acetyl-l-methionine and N-acetyl-l-cysteine, into free amino acids and acetate, playing a critical role in cellular detoxification and amino acid recycling. This enzyme is predominantly expressed in the kidney and liver, with lower levels detected in other tissues. ACY3 belongs to the metallopeptidase M20 family and shares structural homology with other aminoacylases, though its substrate specificity and physiological roles distinguish it from isoforms like ACY1.
Recombinant ACY3 protein is engineered using heterologous expression systems, such as *E. coli* or mammalian cell lines, to enable large-scale production for functional and structural studies. Its recombinant form retains enzymatic activity, allowing researchers to investigate its catalytic mechanism, substrate preferences, and interaction with metal ions (e.g., zinc) essential for activity. Structural studies using recombinant ACY3 have revealed a homodimeric architecture with conserved active-site residues critical for substrate binding and hydrolysis.
Research on ACY3 has gained attention due to its potential links to metabolic disorders, neurodegenerative conditions, and cancer. Aberrant ACY3 expression has been observed in certain tumors, suggesting a role in modulating cellular metabolism or oxidative stress. Additionally, genetic variants in *ACY3* are being explored for associations with neurological phenotypes. Recombinant ACY3 serves as a tool for drug discovery, enzyme replacement therapy, and biomarker development, bridging gaps in understanding its biological significance and therapeutic potential.
Overall, ACY3 recombinant protein is a vital resource for decoding its metabolic functions and translational applications in human health and disease.
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