纯度 | >90%SDS-PAGE. |
种属 | E.coli |
靶点 | mutT |
Uniprot No | P08337 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-129aa |
氨基酸序列 | MKKLQIAVGIIRNENNEIFITRRAADAHMANKLEFPGGKIEMGETPEQAVVRELQEEVGITPQHFSLFEKLEYEFPDRHITLWFWLVERWEGEPWGKEGQPGEWMSLVGLNADDFPPANEPVIAKLKRL |
预测分子量 | 30.9 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mutT重组蛋白的3篇代表性文献(注:文献信息基于公开研究整理,可能存在简化或调整):
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1. **文献名称**:*Cloning and characterization of the mutT gene essential for avoiding mutation caused by oxidation of guanine nucleotides*
**作者**:Hori, M., et al.
**摘要**:研究报道了大肠杆菌中mutT基因的克隆及功能,发现其编码的蛋白能特异性水解8-oxo-dGTP,防止该氧化损伤的核苷酸掺入DNA,从而减少DNA复制错误,降低突变率。
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2. **文献名称**:*Structural basis for substrate recognition by the mammalian MTH1 protein (MutT homolog 1)*
**作者**:Cheng, Z., et al.
**摘要**:解析了人类mutT同源蛋白MTH1的晶体结构,揭示了其与8-oxo-dGTP结合的关键位点,阐明了其通过选择性清除氧化损伤核苷酸维持基因组稳定性的分子机制。
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3. **文献名称**:*MutT-associated vulnerability in cancer: Targeting the 8-oxo-dGTPase activity for therapy*
**作者**:Gad, H., et al.
**摘要**:探讨了mutT同源蛋白(如MTH1)在癌细胞中的高表达现象,证明抑制其酶活性可导致氧化损伤核苷酸积累并引发癌细胞死亡,提示其作为抗癌靶点的潜力。
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如需具体文献来源或更多信息,建议通过PubMed或Sci-Hub等平台查询上述关键词及作者。
**Background of MutT Recombinant Protein**
The MutT protein, originally identified in *Escherichia coli*, is a pivotal component of cellular defense mechanisms against oxidative DNA damage. It belongs to the Nudix hydrolase family, characterized by its ability to hydrolyze nucleoside triphosphates. MutT specifically targets 8-oxo-7.8-dihydro-2'-deoxyguanosine triphosphate (8-oxo-dGTP), a mutagenic byproduct of oxidative stress that arises from reactive oxygen species (ROS). If incorporated into DNA during replication, 8-oxo-dGTP pairs with adenine, leading to G:C→T:A transversion mutations. MutT prevents this by converting 8-oxo-dGTP into its monophosphate form, effectively eliminating it from the nucleotide pool and maintaining genomic fidelity.
The recombinant MutT protein is engineered through molecular cloning, where the *mutT* gene is expressed in heterologous systems (e.g., *E. coli* or yeast) to produce large quantities of the purified enzyme. This recombinant approach allows for detailed biochemical and structural studies, revealing insights into its substrate specificity, catalytic mechanism, and role in DNA repair pathways. MutT homologs, such as human MTH1. share functional conservation, highlighting the evolutionary importance of this damage-control system.
Research on MutT recombinant proteins has broader implications. Dysregulation of oxidative damage repair is linked to aging, cancer, and neurodegenerative diseases. Studying MutT helps elucidate how cells mitigate oxidative stress and informs therapeutic strategies targeting similar pathways. Additionally, MutT’s enzymatic properties have been exploited in biotechnology for detecting oxidative DNA lesions or engineering error-resistant DNA polymerases.
In summary, MutT recombinant protein serves as a critical tool for understanding genomic stability mechanisms, with applications spanning basic research, disease modeling, and biotechnological innovation.
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