| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PRIM1 |
| Uniprot No | P49642 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-420aa |
| 氨基酸序列 | METFDPTELPELLKLYYRRLFPYSQYYRWLNYGGVIKNYFQHREFSFTLKDDIYIRYQSFNNQSDLEKEMQKMNPYKIDIGAVYSHRPNQHNTVKLGAFQAQEKELVFDIDMTDYDDVRRCCSSADICPKCWTLMTMAIRIIDRALKEDFGFKHRLWVYSGRRGVHCWVCDESVRKLSSAVRSGIVEYLSLVKGGQDVKKKVHLSEKIHPFIRKSINIIKKYFEEYALVNQDILENKESWDKILALVPETIHDELQQSFQKSHNSLQRWEHLKKVASRYQNNIKNDKYGPWLEWEIMLQYCFPRLDINVSKGINHLLKSPFSVHPKTGRISVPIDLQKVDQFDPFTVPTISFICRELDAISTNEEEKEENEAESDVKHRTRDYKKTSLAPYVKVFEHFLENLDKSRKGELLKKSDLQKDF |
| 预测分子量 | 65.9 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PRIM1重组蛋白的3篇代表性文献，按作者和摘要内容概括整理：
1. **"Recombinant human DNA primase: expression, purification, and functional characterization"**
*作者：Kuchta et al.*
**摘要**：研究通过大肠杆菌系统重组表达并纯化人源PRIM1蛋白，验证其与DNA聚合酶α的相互作用及在引物合成中的催化活性，为体外复制系统提供功能分析基础。
2. **"Structural basis of the human primase interaction with DNA polymerase α"**
*作者：Baranovskiy et al.*
**摘要**：解析PRIM1与DNA聚合酶α亚基复合体的晶体结构，揭示重组PRIM1在复制起始中的构象变化及其与聚合酶协同作用的分子机制。
3. **"DNA primase subunit 1 expression in cancer: implications for replication stress"**
*作者：Stucky et al.*
**摘要**：利用重组PRIM1蛋白模型，探讨其在肿瘤细胞中的过表达现象，揭示PRIM1异常导致复制压力及基因组不稳定的潜在病理机制。
*注：文献为虚拟示例，实际引用需根据具体研究需求检索数据库(如PubMed)。*
PRIM1 (DNA primase subunit 1) is a critical catalytic component of the DNA primase complex, essential for initiating DNA synthesis in eukaryotic cells. As part of the heterodimeric primase complex (PRIM1-PRIM2), it synthesizes short RNA primers required for DNA polymerases to elongate during replication. These primers provide free 3'-OH groups that allow DNA polymerase α to begin synthesizing the leading and lagging strands. PRIM1 contains conserved primase and zinc-binding domains responsible for its RNA polymerase activity and template recognition.
Recombinant PRIM1 protein is produced through biotechnological methods, often using bacterial (e.g., *E. coli*) or mammalian expression systems. This engineered protein retains enzymatic activity while offering high purity and consistency for research applications. Its production typically involves affinity chromatography (e.g., His-tag purification) followed by functional validation through primer synthesis assays.
Studies of PRIM1 have revealed its role in replication fidelity, cell cycle progression, and cancer biology. Dysregulation of PRIM1 is linked to genomic instability and tumorigenesis, with overexpression observed in various cancers (e.g., breast, liver), making it a potential therapeutic target. Researchers use recombinant PRIM1 to investigate replication mechanisms, screen primase inhibitors, and analyze protein interactions within the replisome. Structural studies employing recombinant PRIM1 have advanced understanding of primase architecture and catalytic mechanisms.
Current challenges include optimizing recombinant PRIM1's stability *in vitro* and mimicking its native interaction with PRIM2 and polymerase α. Ongoing research explores its potential as a biomarker and target for anticancer drugs, particularly in replication-stress-prone malignancies. The development of PRIM1-specific inhibitors could provide new strategies to selectively disrupt cancer cell proliferation.
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