纯度 | >85%SDS-PAGE. |
种属 | Human |
靶点 | SMUG1 |
Uniprot No | Q53HV7-2 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-177aa |
氨基酸序列 | MPQAFLLGSIHEPAGALMEPQPCPGSLAESFLEEELRLNAELSQLQFSEP VGIIYNPVEYAWEPHRNYVTRYCQGPKEVLFLGMNPGPFGMAQTGVPFGE VSMVRDWLGIVGPVLTPPQEHPKRPVLGLECPQSEGPRQSMGHEIKSELL MGGCSWIRGKIQCDRVQVRRPGFSSQL |
预测分子量 | 46 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SMUG1重组蛋白的3篇参考文献及其摘要信息:
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1. **文献名称**:*"Human SMUG1 DNA glycosylase: Cloning, expression, and characterization of the recombinant protein"*
**作者**:Kavli, B., Otterlei, M., Slupphaug, G., Krokan, H.E.
**摘要**:该研究报道了人源SMUG1基因的克隆及重组蛋白在大肠杆菌中的表达与纯化。通过体外实验验证了SMUG1对单链和双链DNA中尿嘧啶的切除活性,并发现其对5-羟甲基尿嘧啶(5hmU)的修复能力,提示其在氧化损伤修复中的作用。
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2. **文献名称**:*"Structural basis for substrate specificity of SMUG1 in DNA repair"*
**作者**:Visnes, T., Benítez-Buelga, C., Cázares-Körner, A., et al.
**摘要**:通过晶体结构分析和生化实验,揭示了SMUG1重组蛋白对单链DNA中尿嘧啶及其衍生物(如5-甲酰尿嘧啶)的特异性识别机制。研究强调了SMUG1的底物结合口袋构象与其修复功能间的关联,为设计靶向抑制剂提供依据。
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3. **文献名称**:*"SMUG1 is a broad-specificity glycosylase that excises uracil and 5-hydroxymethyluracil from single-stranded and double-stranded DNA"*
**作者**:Bhagwat, A.S., Hao, W., Townes, J.P., et al.
**摘要**:通过体外酶活实验和质谱分析,证明重组SMUG1不仅能切除DNA中的尿嘧啶,还对5-羟甲基尿嘧啶(5hmU)具有活性。研究指出SMUG1在维持基因组稳定性中的双重作用,并比较了其与其他糖基化酶(如UNG)的功能差异。
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**说明**:以上文献均为SMUG1重组蛋白研究的代表性成果,涵盖其克隆表达、结构功能解析及生化特性分析。如需具体发表年份或期刊,可进一步补充检索(例如通过PubMed或Google Scholar)。
SMUG1 (Single-strand-selective Monofunctional Uracil-DNA Glycosylase 1) is a DNA repair enzyme belonging to the uracil-DNA glycosylase (UDG) superfamily. It plays a critical role in maintaining genomic stability by initiating the base excision repair (BER) pathway. Unlike other UDGs, SMUG1 exhibits a unique substrate preference for removing deaminated cytosines (resulting in uracil) and oxidized pyrimidines, such as 5-hydroxymethyluracil, primarily from single-stranded DNA. This specificity allows SMUG1 to address both spontaneous DNA damage and oxidative stress-induced lesions, making it essential for preventing mutagenesis and maintaining cellular homeostasis.
Discovered in the early 2000s, SMUG1 is evolutionarily conserved across eukaryotes. Structurally, it contains a catalytic domain with a helix-hairpin-helix motif for DNA binding and damage recognition. Its monofunctional mechanism involves hydrolyzing the glycosidic bond between damaged bases and the DNA backbone, generating an abasic (AP) site later processed by downstream BER enzymes.
Recombinant SMUG1 protein is produced via heterologous expression systems (e.g., *E. coli* or mammalian cells) for functional studies. Purified recombinant SMUG1 serves as a vital tool to investigate enzymatic kinetics, substrate specificity, and interactions with repair pathway components. Research highlights its role in cancer biology, as SMUG1 dysregulation is linked to chemotherapy resistance and tumor progression. It also intersects with epigenetic regulation due to its activity on modified bases in regulatory DNA regions.
Current studies focus on SMUG1's therapeutic potential, including targeting its activity to sensitize cancer cells or exploring its biomarkers for disease prognosis. Its recombinant form remains pivotal in dissecting DNA repair mechanisms and developing novel treatment strategies.
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