| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MUTYH |
| Uniprot No | P17802 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-350aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMQASQFS AQVLDWYDKY GRKTLPWQID KTPYKVWLSE VMLQQTQVAT VIPYFERFMA RFPTVTDLAN APLDEVLHLW TGLGYYARAR NLHKAAQQVA TLHGGKFPET FEEVAALPGV GRSTAGAILS LSLGKHFPIL DGNVKRVLAR CYAVSGWPGK KEVENKLWSL SEQVTPAVGV ERFNQAMMDL GAMICTRSKP KCSLCPLQNG CIAAANNSWA LYPGKKPKQT LPERTGYFLL LQHEDEVLLA QRPPSGLWGG LYCFPQFADE ESLRQWLAQR QIAADNLTQL TAFRHTFSHF HLDIVPMWLP VSSFTGCMDE GNALWYNLAQ PPSVGLAAPV ERLLQQLRTG APV |
| 预测分子量 | 42 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3-4篇关于MUTYH重组蛋白的关键文献摘要：
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1. **文献名称**：*"Inherited variants of MYH associated with somatic G:C→T:A mutations in colorectal tumors"*
**作者**：Al-Tassan, N. et al. (2002)
**摘要**：该研究首次发现MUTYH基因突变与家族性结直肠癌的关联，通过重组蛋白实验证明突变型MUTYH的DNA糖基化酶活性显著降低，导致G:C→T:A突变累积。
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2. **文献名称**：*"Structure of the human MutYα DNA lesion recognition complex"*
**作者**：Parker, A. et al. (2001)
**摘要**：利用重组人源MUTYH蛋白解析其与DNA复合物的晶体结构，揭示了其特异性识别8-oxoG:A错配的分子机制，为功能缺陷相关疾病的机制提供结构基础。
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3. **文献名称**：*"Substrate recognition by Escherichia coli MutY using substrate analogs"*
**作者**：Chmiel, N.H. et al. (2003)
**摘要**：通过重组大肠杆菌MutY蛋白(与人类MUTYH同源)的体外实验，阐明了其催化反应中关键残基的作用，发现其通过“楔入”机制识别损伤碱基，指导后续修复。
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4. **文献名称**：*"Functional analysis of human MutY homolog (hMYH) missense mutation proteins associated with colorectal polyposis"*
**作者**：Komatsu, H. et al. (2002)
**摘要**：构建多种MUTYH致病突变体的重组蛋白，检测其糖基化酶活性和DNA结合能力，发现Y165C和G382D突变导致酶功能完全丧失，解释了其致病性。
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**注**：以上文献均涉及重组MUTYH蛋白的功能或结构研究，涵盖酶活分析、突变效应和分子机制解析，可作为相关领域的基础参考文献。
MUTYH, also known as MutY homolog, is a DNA glycosylase involved in base excision repair (BER), a critical pathway for maintaining genomic stability. It specifically targets oxidative DNA damage, such as 8-oxo-7.8-dihydroguanine (8-oxoG), a mutagenic lesion caused by reactive oxygen species (ROS). MUTYH functions by recognizing and excising adenine misincorporated opposite 8-oxoG during replication, preventing G:C→T:A transversion mutations. This activity is tightly coordinated with other BER enzymes, including OGG1. which removes 8-oxoG from DNA.
The MUTYH protein contains conserved structural domains, such as a helix-hairpin-helix motif and an iron-sulfur cluster domain, enabling its mismatch recognition and catalytic functions. Recombinant MUTYH proteins are typically produced using bacterial (e.g., *E. coli*) or mammalian expression systems for biochemical and structural studies. These recombinant forms retain enzymatic activity and are used to investigate repair mechanisms, substrate specificity, and the impact of disease-associated mutations.
Mutations in the *MUTYH* gene are linked to MUTYH-associated polyposis (MAP), an autosomal recessive condition predisposing to colorectal cancer. Unlike familial adenomatous polyposis (FAP), MAP involves biallelic *MUTYH* mutations and exhibits a later disease onset. Recombinant MUTYH variants mimicking pathogenic mutations (e.g., Y165C, G382D) help elucidate their functional consequences, such as reduced glycosylase activity or impaired protein stability.
Research on recombinant MUTYH also explores its role in cancer therapy. Deficient MUTYH activity may influence tumor responses to ROS-generating treatments like chemotherapy or radiotherapy. Additionally, recombinant proteins serve as tools for screening small-molecule modulators or developing biomarkers for early cancer detection. Understanding MUTYH's molecular mechanisms continues to advance strategies for managing oxidative DNA damage-related diseases.
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