| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NAT5 |
| Uniprot No | Q9GZZ1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-169aa |
| 氨基酸序列 | MKGSRIELGDVTPHNIKQLKRLNQVIFPVSYNDKFYKDVLEVGELAKLAYFNDIAVGAVCCRVDHSQNQKRLYIMTLGCLAPYRRLGIGTKMLNHVLNICEKDGTFDNIYLHVQISNESAIDFYRKFGFEIIETKKNYYKRIEPADAHVLQKNLKVPSGQNADVQKTDN |
| 预测分子量 | 46.4 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NAT5重组蛋白的虚构参考文献示例(仅供格式参考)：
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1. **文献名称**: *Expression and Functional Analysis of Recombinant NAT5 Acetyltransferase in E. coli*
**作者**: Zhang, L. et al.
**摘要**: 本研究报道了在大肠杆菌中高效表达NAT5重组蛋白的优化方法，并通过亲和层析纯化获得高纯度蛋白。酶活性实验表明，重组NAT5对组蛋白H4的N端乙酰化具有特异性，为研究其表观遗传调控机制提供了工具。
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2. **文献名称**: *Structural Insights into NAT5 Catalytic Mechanism by Cryo-EM*
**作者**: Patel, R.K. & Müller, J.
**摘要**: 通过冷冻电镜解析了NAT5重组蛋白的3.2 Å三维结构，揭示了其底物结合口袋的关键氨基酸残基，并提出了乙酰辅酶A转移的分子机制，为靶向NAT5的药物设计奠定基础。
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3. **文献名称**: *NAT5 Recombinant Protein as a Potential Biomarker in Colorectal Cancer*
**作者**: Chen, Y. et al.
**摘要**: 研究发现NAT5重组蛋白在结直肠癌细胞中表达异常升高，体外实验证实其通过乙酰化调控Wnt/β-catenin信号通路，提示其可作为癌症诊断和治疗的新靶点。
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4. **文献名称**: *High-Throughput Screening of NAT5 Inhibitors Using Recombinant Protein Assays*
**作者**: Gupta, S. et al.
**摘要**: 基于NAT5重组蛋白建立高通量酶活性筛选平台，从化合物库中鉴定出两种小分子抑制剂，显著抑制癌细胞增殖，为开发新型抗癌药物提供候选分子。
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注：以上文献信息为虚构示例，实际研究中需引用真实发表的学术论文。
**Background of NAT5 Recombinant Protein**
NAT5 (N-acetyltransferase 5), also known as NAA50 or San, is a member of the N-terminal acetyltransferase (NAT) family, which catalyzes the acetylation of proteins at their N-termini. This post-translational modification plays a critical role in regulating protein stability, localization, and interactions. NAT5 is distinct from other NATs due to its unique substrate specificity and evolutionary conservation across eukaryotes. It primarily acetylates the α-amino group of nascent polypeptide chains, particularly those starting with methionine followed by hydrophobic residues, influencing cellular processes such as chromosome segregation, DNA repair, and cell cycle progression.
The recombinant NAT5 protein is produced using genetic engineering techniques, often expressed in *E. coli* or yeast systems, enabling large-scale purification for functional studies. Its recombinant form retains enzymatic activity, making it a valuable tool for *in vitro* assays, structural studies, and drug discovery. Research has linked NAT5 dysregulation to diseases, including cancers and neurodevelopmental disorders, highlighting its potential as a therapeutic target. For instance, aberrant NAT5 expression may disrupt mitotic fidelity, contributing to genomic instability in tumors.
Recent advances in structural biology, such as cryo-EM and X-ray crystallography, have elucidated NAT5's interaction with ribosomes and substrate proteins, shedding light on its catalytic mechanism. Additionally, studies exploring NAT5's role in aging and stress responses underscore its broader biological significance. The availability of recombinant NAT5 continues to drive innovations in understanding N-terminal acetylation's functional diversity and its implications in health and disease.
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