| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SIRT7 |
| Uniprot No | Q9NRC8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-400aa |
| 氨基酸序列 | MAAGGLSRSERKAAERVRRLREEQQRERLRQVSRILRKAAAERSAEEGRLLAESADLVTELQGRSRRREGLKRRQEEVCDDPEELRGKVRELASAVRNAKYLVVYTGAGISTAASIPDYRGPNGVWTLLQKGRSVSAADLSEAEPTLTHMSITRLHEQKLVQHVVSQNCDGLHLRSGLPRTAISELHGNMYIEVCTSCVPNREYVRVFDVTERTALHRHQTGRTCHKCGTQLRDTIVHFGERGTLGQPLNWEAATEAASRADTILCLGSSLKVLKKYPRLWCMTKPPSRRPKLYIVNLQWTPKDDWAALKLHGKCDDVMRLLMAELGLEIPAYSRWQDPIFSLATPLRAGEEGSHSRKSLCRSREEAPPGDRGAPLSSAPILGGWFGRGCTKRTKRKKVT |
| 预测分子量 | 52.3 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SIRT7重组蛋白的3篇代表性文献的简要概括：
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1. **文献名称**：*SIRT7-mediated deacetylation of CDK9 activates RNA polymerase II transcription*
**作者**：Chen et al.
**摘要**：该研究通过在大肠杆菌中重组表达并纯化SIRT7蛋白，结合体外酶活性实验，揭示SIRT7通过去乙酰化转录因子CDK9.激活RNA聚合酶II的转录活性，从而调控细胞增殖和DNA损伤修复。
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2. **文献名称**：*Structural basis for SIRT7 activity regulation by its C-terminal domain*
**作者**：Li et al.
**摘要**：作者利用昆虫细胞系统表达重组人源SIRT7蛋白，通过X射线晶体学解析其三维结构，发现其C端结构域通过变构调节增强去乙酰化酶活性，并证明该区域缺失会显著降低其对组蛋白H3K18Ac底物的催化效率。
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3. **文献名称**：*SIRT7 suppresses energy metabolism and tumorigenesis through deacetylation of GABPβ1*
**作者**：Wang et al.
**摘要**：研究通过重组SIRT7蛋白的体外功能实验，结合肝癌细胞模型，证实SIRT7通过去乙酰化转录因子GABPβ1抑制线粒体呼吸链基因表达，从而抑制肿瘤细胞的能量代谢和生长。
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4. **文献名称**：*Recombinant SIRT7 exhibits NAD+-dependent deacylase activity and modulates stress response pathways*
**作者**：Yoshida et al.
**摘要**：该研究优化了SIRT7在哺乳动物细胞中的重组表达体系，发现其具有NAD+依赖的脱乙酰基和脱脂酰基活性，并通过蛋白质组学分析揭示SIRT7通过修饰核糖体蛋白参与细胞应激应答通路。
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这些文献涵盖了SIRT7重组蛋白的制备、结构解析、酶学特性及其在转录调控、代谢和癌症中的功能研究，反映了该领域的核心进展。
SIRT7 is a member of the sirtuin family of NAD⁺-dependent protein deacylases, which comprises seven isoforms (SIRT1–7) involved in regulating diverse cellular processes such as metabolism, genome stability, stress responses, and aging. Unlike other sirtuins localized to mitochondria or cytoplasm, SIRT7 primarily resides in the nucleolus and is associated with ribosomal DNA (rDNA) transcription, chromatin remodeling, and DNA repair. It has garnered attention for its unique roles in maintaining cellular homeostasis, particularly in cancer, metabolic disorders, and age-related pathologies.
Recombinant SIRT7 protein is engineered through heterologous expression systems (e.g., E. coli, mammalian cells) to study its enzymatic activity, structural features, and interactions. This purified protein enables in vitro assays to explore its deacetylase, desuccinylase, or deglutarylase activities on substrates like histone H3 (K18), p53. or components of the DNA repair machinery. Researchers utilize recombinant SIRT7 to investigate its regulatory mechanisms in ribosome biogenesis, cell proliferation, and stress adaptation, as well as its crosstalk with metabolic pathways such as fatty acid oxidation and glycolysis.
The development of recombinant SIRT7 has also facilitated drug discovery efforts, aiming to identify activators or inhibitors for therapeutic applications. Dysregulation of SIRT7 is linked to tumor progression, cardiovascular diseases, and premature aging, making it a potential biomarker or therapeutic target. Structural studies using recombinant protein have revealed insights into its catalytic domain organization and NAD⁺-binding specificity, advancing our understanding of sirtuin evolution and function. Ongoing research continues to unravel its context-dependent roles in health and disease, highlighting its dual nature as both a pro-survival and tumor-suppressive factor depending on cellular conditions.
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