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Recombinant Human SMUG1 protein

  • 中文名: 单链选择性单功能尿嘧啶DNA糖基化酶1(SMUG1)重组蛋白
  • 别    名: SMUG1;Single-strand selective monofunctional uracil DNA glycosylase
货号: PA1000-2959
Price: ¥询价
数量:
大包装询价

产品详情

纯度>85%SDS-PAGE.
种属Human
靶点SMUG1
Uniprot NoQ53HV7-2
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.

参考文献

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)。

背景信息

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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