| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | APOBEC3C |
| Uniprot No | Q9NRW3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-190aa |
| 氨基酸序列 | MNPQIRNPMKAMYPGTFYFQFKNLWEANDRDETWLCFTVEGIKRRSVVSWKTGVFRNQVDSETHCHAERCFLSWFCDDILSPNTKYQVTWYTSWSPCPDCAGEVAEFLARHSNVNLTIFTARLYYFQYPCYQEGLRSLSQEGVAVEIMDYEDFKYCWENFVYNDNEPFKPWKGLKTNFRLLKRRLRESLQ |
| 预测分子量 | 49.8 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APOBEC3C重组蛋白的3篇示例参考文献(注：以下内容为虚构示例，仅供参考格式)：
1. **文献名称**：*Structural and functional characterization of recombinant APOBEC3C as a restriction factor against HIV-1*
**作者**：Smith J, et al.
**摘要**：该研究通过大肠杆菌表达系统纯化重组APOBEC3C蛋白，分析了其胞苷脱氨酶活性及抗HIV-1的机制，证实其通过诱导病毒DNA超突变抑制病毒复制。
2. **文献名称**：*APOBEC3C crystal structure reveals insights into DNA binding and catalytic activity*
**作者**：Zhang Y, Wang L, et al.
**摘要**：作者解析了重组APOBEC3C的晶体结构，揭示了其锌指结构域和底物结合位点的关键氨基酸残基，为设计靶向该蛋白的抑制剂提供结构基础。
3. **文献名称**：*Comparative analysis of APOBEC3 family members in retroelement suppression*
**作者**：Lee S, et al.
**摘要**：研究比较了重组APOBEC3C与其他家族蛋白(如APOBEC3G)的抗逆转录转座子活性，发现APOBEC3C对LINE-1元件的抑制作用依赖于其寡聚化能力。
(如需真实文献，建议在PubMed或Google Scholar中检索关键词“APOBEC3C recombinant protein”)
APOBEC3C (Apolipoprotein B mRNA-editing enzyme catalytic subunit 3C) is a member of the APOBEC3 family of cytidine deaminases, which play critical roles in innate immunity by restricting viral infections and retrotransposon activity. These enzymes catalyze the deamination of cytidine to uridine in single-stranded DNA, introducing mutations that disrupt viral genome replication or retrotransposon propagation. APOBEC3C, specifically, has been implicated in restricting HIV-1. hepatitis B virus (HBV), and other pathogens, though its antiviral potency varies across primate species due to evolutionary adaptations.
Recombinant APOBEC3C protein is engineered for in vitro studies to dissect its biochemical properties, structural features, and interactions with viral or cellular factors. It is typically produced using bacterial (e.g., E. coli) or mammalian expression systems, followed by purification via affinity tags (e.g., His-tag) and chromatographic techniques. Structural studies reveal its conserved zinc-coordinating catalytic domain and unique loop regions critical for substrate recognition and activity regulation.
Research on recombinant APOBEC3C has advanced understanding of its dual roles: as a host defense protein and a potential contributor to genomic instability in cancers. Its hypermutation activity, while protective against viruses, may also cause off-target DNA edits in human cells, linking it to carcinogenic mutagenesis. Additionally, APOBEC3C's ability to bind RNA and regulate viral reverse transcripts highlights its multifunctionality. Current challenges include optimizing its enzymatic activity in vitro, developing delivery systems for therapeutic applications, and elucidating mechanisms that balance its protective versus mutagenic effects. These studies hold promise for antiviral drug design and precision genome-editing tools.
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