| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | OGG1 |
| Uniprot No | O15527 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-345aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHTGSMPARALLPRRMGHRTLASTPALWASIP CPRSELRLDLVLPSGQSFRWREQSPAHWSGVLADQVWTLTQTEEQLHCTV YRGDKSQASRPTPDELEAVRKYFQLDVTLAQLYHHWGSVDSHFQEVAQKF QGVRLLRQDPIECLFSFICSSNNNIARITGMVERLCQAFGPRLIQLDDVT YHGFPSLQALAGPEVEAHLRKLGLGYRARYVSASARAILEEQGGLAWLQQ LRESSYEEAHKALCILPGVGTKVADCICLMALDKPQAVPVDVHMWHIAQR DYSWHPTTSQAKGPSPQTNKELGNFFRSLWGPYAGWAQAVLFSADLRQCR HAQEPPAKRRKGSKGPEG |
| 预测分子量 | 41 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条关于OGG1重组蛋白的参考文献示例(内容为模拟概括，非真实文献)：
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1. **标题**：*Cloning and characterization of human OGG1 DNA glycosylase*
**作者**：Bjørås M, et al.
**摘要**：研究报道了人源OGG1重组蛋白的克隆与功能分析，证实其特异性识别并切除8-氧鸟嘌呤(8-oxoG)损伤，通过大肠杆菌表达系统纯化蛋白并验证其修复活性。
2. **标题**：*Recombinant OGG1 protein repairs oxidative DNA damage in mammalian cells*
**作者**：Rosenquist TA, et al.
**摘要**：利用重组OGG1蛋白在体外和细胞模型中验证其修复8-oxoG的能力，证明其通过碱基切除修复(BER)途径减少氧化应激诱导的DNA突变。
3. **标题**：*Structural and functional analysis of OGG1 variants using recombinant protein expression*
**作者**：Dizdaroglu M, et al.
**摘要**：通过重组蛋白技术表达多种OGG1突变体，解析其晶体结构并评估不同突变对酶活性的影响，揭示关键氨基酸在底物识别中的作用。
4. **标题**：*Yeast homolog of OGG1: A comparative study with recombinant proteins*
**作者**：Boiteux S, et al.
**摘要**：比较酵母与人源OGG1重组蛋白的酶动力学差异，发现两者对8-oxoG的修复效率及底物特异性存在物种特异性差异。
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注：以上文献信息为模拟概括，实际引用时需以真实发表的论文为准。
**Background of OGG1 Recombinant Protein**
OGG1 (8-oxoguanine DNA glycosylase 1) is a critical enzyme in the base excision repair (BER) pathway, responsible for repairing oxidative DNA damage. It specifically recognizes and excises 8-oxo-7.8-dihydroguanine (8-oxoG), a mutagenic lesion caused by reactive oxygen species (ROS) that arises during normal cellular metabolism or environmental stress. Failure to repair 8-oxoG can lead to G:C to T:A transversion mutations, contributing to genomic instability and diseases such as cancer, neurodegeneration, and aging-related disorders.
Recombinant OGG1 protein is produced using genetic engineering techniques, often expressed in *E. coli*, insect, or mammalian cell systems. This allows for large-scale production of high-purity, active OGG1 for research and therapeutic applications. The recombinant protein retains the functional domains of native OGG1. including a DNA-binding domain for lesion recognition and a glycosylase/AP lyase domain for cleaving damaged bases.
Structurally, OGG1 exists in multiple isoforms (e.g., OGG1-1a and OGG1-2a), differing in subcellular localization—nuclear or mitochondrial—highlighting its role in safeguarding both genomic and mitochondrial DNA. Studies using recombinant OGG1 have elucidated its kinetics, substrate specificity, and interactions with other BER proteins.
In research, recombinant OGG1 is used to study oxidative stress mechanisms, evaluate DNA repair capacity in disease models, and screen potential drugs targeting BER. It also serves as a tool for detecting 8-oxoG lesions in DNA, aiding biomarker development. Therapeutically, enhancing OGG1 activity is explored to mitigate oxidative damage in age-related diseases, while inhibitors are investigated for sensitizing cancer cells to radiation or chemotherapy.
Overall, OGG1 recombinant protein is indispensable for advancing our understanding of DNA repair biology and developing strategies to combat oxidative stress-associated pathologies.
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