| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | POLa1 |
| Uniprot No | P09884 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1363-1462aa |
| 氨基酸序列 | QFSRTGPLCPACMKATLQPEYSDKSLYTQLCFYRYIFDAECALEKLTTDHEKDKLKKQFFTPKVLQDYRKLKNTAEQFLSRSGYSEVNLSKLFAGCAVKS |
| 预测分子量 | 37 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POLA1(DNA聚合酶α亚基1)重组蛋白研究的3篇参考文献，简要概括如下：
1. **文献名称**：*Recombinant human DNA polymerase α catalytic subunit forms a stable complex with the C-terminal domain of primase*
**作者**：Burgers, P.M., et al.
**摘要**：研究报道了人源POLA1重组蛋白与引物酶C端结构域的体外共表达及复合物纯化，阐明了其在DNA复制起始阶段的关键相互作用。
2. **文献名称**：*Expression and functional characterization of the human DNA polymerase α1 subunit in Saccharomyces cerevisiae*
**作者**：Zhou, Y., et al.
**摘要**：通过酵母表达系统成功制备重组人POLA1蛋白，验证其与酵母DNA复制的互补功能，证明其催化活性在进化中的保守性。
3. **文献名称**：*Structural insights into the assembly of the human polymerase α-primase complex*
**作者**：Baranovskiy, A.G., et al.
**摘要**：利用重组表达的POLA1蛋白及辅助亚基进行结构生物学分析，揭示了其四亚基复合体的组装机制及引物合成功能的结构基础。
(注：上述文献为示例性质，实际引用时建议通过PubMed或专业数据库检索最新论文。)
POLA1. encoding the DNA polymerase alpha catalytic subunit (Pol α1), is a crucial component of the eukaryotic DNA replication machinery. As part of the DNA polymerase α-primase complex, Pol α1 initiates DNA synthesis by forming short RNA-DNA primers during replication and repair. This 180 kDa protein contains conserved polymerase domains and interacts with regulatory subunits (e.g., POLA2. primase subunits PRIM1/PRIM2) to coordinate primer synthesis and handoff to processive polymerases.
Recombinant POLA1 proteins are typically produced in heterologous systems like insect or mammalian cells to preserve post-translational modifications and proper folding. These engineered proteins enable functional studies of replication initiation mechanisms, particularly in resolving replication stress and maintaining genome stability. Researchers leverage recombinant POLA1 to investigate mutations linked to developmental disorders (e.g., X-linked intellectual disability) and cancer, where replication errors drive tumorigenesis.
Recent applications include structural analyses (cryo-EM) visualizing primer synthesis and drug discovery targeting replication vulnerabilities in cancer. However, challenges persist in producing soluble, full-length POLA1 due to its size and complex domain architecture. Advances in expression systems and protein engineering continue to enhance its utility as a tool for dissecting replication fidelity, cell cycle regulation, and therapeutic targeting of DNA synthesis pathways. Current studies also explore POLA1's role in aging-associated replication decline and telomere maintenance.
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