| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | REV1 |
| Uniprot No | Q9UBZ9-1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 51-256aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGVAIYVNGY TDPSAEELRK LMMLHGGQYH VYYSRSKTTH IIATNLPNAK IKELKGEKVI RPEWIVESIK AGRLLSYIPY QLYTKQSSVQ KGLSFNPVCR PEDPLPGPSN IAKQLNNRVN HIVKKIETEN EVKVNGMNSW NEEDENNDFS FVDLEQTSPG RKQNGIPHPR GSTAIFNGHT PSSNGALKTQ DCLVPMVNSV ASRLSPA |
| 预测分子量 | 25 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篇关于REV1重组蛋白的参考文献简列：
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1. **"Crystal structure of human REV1 in complex with a DNA polymerase ζ fragment"**
*作者：Xie, W., et al. (2010)*
摘要：解析了人源REV1蛋白与DNA聚合酶ζ(Polζ)相互作用的晶体结构，揭示了REV1通过C端结构域招募Polζ以协调跨损伤DNA合成的分子机制。
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2. **"REV1 promotes polymerase η-dependent translesion synthesis in human cells"**
*作者：Bianchi, J.J., et al. (2013)*
摘要：研究显示重组表达的REV1通过其泛素结合结构域(UBM)与单链DNA结合，促进DNA损伤位点招募Polη等TLS聚合酶，增强细胞对紫外辐射的抗性。
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3. **"Targeting REV1 disrupts mutagenic translesion synthesis in melanoma"**
*作者：Wojtaszek, J.L., et al. (2019)*
摘要：利用重组REV1蛋白筛选小分子抑制剂，发现抑制REV1与TLS聚合酶的互作可减少黑色素瘤细胞的突变累积，为癌症治疗提供新靶点。
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(注：以上文献信息为模拟示例，实际引用需核对真实数据库。)
**Background of REV1 Recombinant Protein**
REV1 is a specialized DNA polymerase belonging to the Y-family of translesion DNA synthesis (TLS) enzymes, which play a critical role in bypassing DNA lesions during replication. Discovered as a key mediator of error-prone repair, REV1 facilitates replication past damaged bases that stall high-fidelity polymerases, thereby maintaining genome stability and cell survival under genotoxic stress. Structurally, REV1 contains a unique N-terminal ubiquitin-binding domain, a central catalytic core, and a C-terminal scaffold region that interacts with other TLS polymerases (e.g., Pol ζ, Pol η). Unlike most polymerases, REV1 primarily functions as a deoxycytidyl transferase, preferentially inserting dCMP opposite DNA lesions or abasic sites, though its scaffolding role in coordinating TLS is equally vital.
REV1’s recombinant form is generated via heterologous expression systems (e.g., *E. coli* or mammalian cells) for biochemical and structural studies. Recombinant REV1 enables detailed analysis of its enzymatic activity, lesion-bypass mechanisms, and interactions with DNA/protein partners. Research highlights its dual role: while TLS promotes cell survival, dysregulation contributes to mutagenesis and cancer progression. REV1 overexpression is linked to chemotherapy resistance in tumors, making it a potential therapeutic target.
Studies using recombinant REV1 have also clarified its regulation, including post-translational modifications (e.g., ubiquitination, phosphorylation) and spatial-temporal control during the cell cycle. Furthermore, structural insights from recombinant protein crystallography have identified functional domains critical for DNA binding and polymerase recruitment.
In summary, REV1 recombinant protein serves as a vital tool for dissecting TLS mechanisms, cancer biology, and developing strategies to overcome drug resistance, underscoring its importance in DNA repair research and translational oncology.
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