| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | APOBEC3A |
| Uniprot No | P31941 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-199aa |
| 氨基酸序列 | MEASPASGPRHLMDPHIFTSNFNNGIGRHKTYLCYEVERLDNGTSVKMDQHRGFLHNQAKNLLCGFYGRHAELRFLDLVPSLQLDPAQIYRVTWFISWSPCFSWGCAGEVRAFLQENTHVRLRIFAARIYDYDPLYKEALQMLRDAGAQVSIMTYDEFKHCWDTFVDHQGCPFQPWDGLDEHSQALSGRLRAILQNQGN |
| 预测分子量 | 24.5 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APOBEC3A重组蛋白的代表性文献示例(注：内容为模拟概括，实际文献请通过学术数据库核实)：
1. **"APOBEC3A is a potent inhibitor of adeno-associated virus and retrotransposons"**
*作者：Bogerd, H.P. et al.*
摘要：该研究通过体外表达重组APOBEC3A蛋白，证实其能通过胞嘧啶脱氨酶活性有效抑制腺相关病毒(AAV)和逆转录转座子的复制，揭示了其在先天免疫中的新功能。
2. **"Structural basis for targeted DNA cytosine deamination by APOBEC3A"**
*作者：Shi, K. et al.*
摘要：通过X射线晶体学解析了重组APOBEC3A蛋白与DNA复合物的结构，阐明了其特异性识别单链DNA中TC基序并催化胞嘧啶脱氨的分子机制。
3. **"APOBEC3A drives mutagenesis in human cancers through DNA editing"**
*作者：Chan, K. & Gordenin, D.A.*
摘要：利用重组APOBEC3A蛋白进行体外DNA损伤实验，证明其在癌症基因组中产生特征性C>T突变谱，提示其在肿瘤进化中的驱动作用。
4. **"Recombinant APOBEC3A preferentially targets G-quadruplex structures"**
*作者：Chambers, V.S. et al.*
摘要：研究发现重组APOBEC3A蛋白对富含G4四链体结构的DNA区域表现出更强的结合和脱氨活性，提示其功能可能与基因组非B型结构的调控相关。
(提示：以上为领域典型研究方向示例，实际文献建议通过PubMed/Google Scholar以 "APOBEC3A recombinant" 为关键词检索近年高被引论文)
APOBEC3A (apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3A) is a member of the APOBEC family of cytidine deaminases, which play critical roles in innate immunity by restricting viral infections and maintaining genome integrity. These enzymes catalyze the deamination of cytosine to uracil in single-stranded DNA or RNA, introducing mutations that can disrupt viral replication or trigger DNA damage responses. APOBEC3A, located on chromosome 22. is unique among APOBEC3 proteins due to its potent DNA-editing activity and lack of a conserved C-terminal domain found in other family members (e.g., APOBEC3G). Its expression is typically induced by interferons during viral infections, positioning it as a frontline defense against pathogens like HIV, hepatitis B virus (HBV), and human papillomavirus (HPV).
Recombinant APOBEC3A protein is engineered for in vitro studies to elucidate its structural and functional properties. Produced via heterologous expression systems (e.g., E. coli or mammalian cells), the purified protein retains enzymatic activity, enabling research into its deamination mechanisms, substrate specificity, and interactions with viral or cellular factors. Studies using recombinant APOBEC3A have revealed its role in inducing clustered mutagenesis (e.g., kataegis) in cancer genomes, linking its dysregulation to somatic mutations in malignancies. However, its uncontrolled activity can contribute to genomic instability, highlighting a dual role in both host defense and carcinogenesis. Current research focuses on modulating APOBEC3A activity for therapeutic applications, including antiviral strategies and targeting APOBEC-induced mutagenesis in cancer.
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