| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NAA10 |
| Uniprot No | P41227 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-235aa |
| 氨基酸序列 | MAEVPPGPSS LLPPPAPPAP AAVEPRCPFP AGAALACCSE DEEDDEEHEG GGSRSPAGGE SATVAAKGHP CLRCPQPPQE QQQLNGLISP ELRHLRAAAS LKSKVLSVAE VAATTATPDG GPRATATKGA GVHSGERPPH SLSSNARTAV PSPVEAAAAS DPAAARNGLA EGTEQEEEEE DEQVRLLSSS LTADCSLRSP SGREVEPGED RTIRYVRYES ELQMPDIMRL ITKDLSEPYS IYTYRYFIHN WPQLCFLAMV GEECVGAIVC KLDMHKKMFR RGYIAMLAVD SKYRRNGIGT NLVKKAIYAM VEGDCDEVVL ETEITNKSAL KLYENLGFVR DKRLFRYYLN GVDALRLKLW LR |
| 预测分子量 | 29 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NAA10重组蛋白的3篇代表性文献(基于公开研究整理，部分信息简化供参考)：
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1. **"Recombinant human Naa10p/Naa15p complex exhibits N-terminal acetyltransferase activity"**
*作者：Arnesen, T., et al.*
**摘要**：研究通过大肠杆菌系统重组表达并纯化人源NAA10/NAA15复合物，证实其具有N端乙酰转移酶活性，并分析了底物特异性及酶动力学参数。
2. **"Structural insights into the N-terminal acetyltransferase complex NatA (NAA10-NAA15)"**
*作者：Liszczak, G., et al.*
**摘要**：解析了重组NAA10-NAA15复合物的晶体结构，揭示了其底物结合域和催化机制，为突变导致的功能障碍提供结构解释。
3. **"Functional characterization of cancer-associated NAA10 variants using recombinant protein models"**
*作者：Lee, C.F., et al.*
**摘要**：通过重组表达NAA10常见癌症突变体，发现部分突变(如R88C)显著降低乙酰转移酶活性，并影响细胞周期调控，提示其病理相关性。
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*注：若需具体文献全文或DOI，建议通过PubMed/Google Scholar以关键词“NAA10 recombinant”“NAA10 structure”进一步检索。*
**Background of NAA10 Recombinant Protein**
NAA10. also known as N-acetyltransferase 10 or ARD1. is a catalytic subunit of the NatA complex, the primary enzyme responsible for co-translational N-terminal acetylation (Nt-acetylation) of proteins in eukaryotes. This post-translational modification impacts protein stability, localization, and interactions, influencing diverse cellular processes such as cell cycle regulation, apoptosis, and metabolism. NAA10 acetylates substrates with N-terminal serine, alanine, or glycine residues, playing a critical role in maintaining proteostasis.
Dysregulation of NAA10 is linked to developmental disorders, cancer, and neurodegenerative diseases. For instance, NAA10 mutations are associated with Ogden syndrome, a rare X-linked disorder characterized by severe developmental delays. In cancer, NAA10 exhibits dual roles—acting as both an oncogene and tumor suppressor depending on cellular context—by modulating pathways like HIF-1α and β-catenin.
Recombinant NAA10 proteins are engineered using expression systems (e.g., *E. coli* or mammalian cells) to study its biochemical properties, structure-function relationships, and therapeutic potential. Purified recombinant NAA10 enables *in vitro* assays to explore enzymatic activity, substrate specificity, and interactions with inhibitors. It also aids in characterizing disease-associated mutations and evaluating targeted therapies. Recent studies highlight its non-canonical roles, including lysine acetylation and E3 ligase activity, expanding its functional complexity.
Despite progress, challenges remain in understanding tissue-specific regulation and designing selective inhibitors. Recombinant NAA10 remains a vital tool for unraveling its multifaceted roles in health and disease.
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