| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | OBFC2A |
| Uniprot No | Q96AH0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-204aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMNRVNDP LIFIRDIKPG LKNLNVVFIV LEIGRVTKTK DGHEVRSCKV ADKTGSITIS VWDEIGGLIQ PGDIIRLTRG YASMWKGCLT LYTGRGGELQ KIGEFCMVYS EVPNFSEPNP DYRGQQNKGA QSEQKNNSMN SNMGTGTFGP VGNGVHTGPE SREHQFSHAG RSNGRGLINP QLQGTASNQT VMTTISNGRD PRRAFKR |
| 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. |
以下是关于OBFC2A重组蛋白的3篇参考文献示例(注：文献为虚构示例，仅供格式参考)：
1. **文献名称**：*"Recombinant OBFC2A Protein Expression and Its Role in Single-Strand DNA Binding"*
**作者**：Smith J. et al.
**摘要**：本研究成功在大肠杆菌中表达并纯化了OBFC2A重组蛋白，通过凝胶迁移实验证实其特异性结合单链DNA的能力，并揭示其在DNA复制压力下参与基因组稳定的分子机制。
2. **文献名称**：*"Structural Analysis of OBFC2A-STN1 Complex in Telomere Maintenance"*
**作者**：Lee H. et al.
**摘要**：利用重组OBFC2A与STN1蛋白共表达体系，解析了二者复合物的晶体结构，阐明OBFC2A通过OB结构域介导与STN1的相互作用，从而在端粒保护中发挥关键作用。
3. **文献名称**：*"Functional Characterization of OBFC2A Mutants Using Recombinant Protein Assays"*
**作者**：Zhang Y. et al.
**摘要**：通过体外重组蛋白功能实验，发现OBFC2A的R123A突变体丧失DNA结合活性，证明该位点对其在复制相关DNA损伤修复中的功能至关重要。
如需真实文献，建议通过PubMed或Google Scholar以 **"OBFC2A recombinant protein"** 或 **"OBFC2A AND (expression OR purification)"** 为关键词检索。
The OBFC2A (OB Fold Containing 2A) protein, also known as STN1. is a critical component of the mammalian CST (CTC1-STN1-TEN1) complex, which plays essential roles in genome maintenance and telomere protection. Structurally, OBFC2A contains an oligonucleotide/oligosaccharide-binding (OB) fold domain, a conserved motif enabling interactions with single-stranded DNA (ssDNA). This protein is functionally analogous to the replication protein A (RPA) but operates specifically at telomeres and stalled replication forks.
The CST complex coordinates telomere length regulation by recruiting telomerase and controlling its access to chromosome ends. During DNA replication, OBFC2A facilitates the resolution of replication stress by promoting the restart of stalled forks and preventing excessive resection of damaged DNA. It also collaborates with DNA polymerase α-primase to fill in telomeric ssDNA gaps, ensuring proper C-strand synthesis. Dysregulation of OBFC2A has been linked to telomere dysfunction, genomic instability, and pathologies such as cancer and the rare genetic disorder Coats plus syndrome.
Recombinant OBFC2A protein is typically produced using bacterial or eukaryotic expression systems for in vitro studies. Its purified form enables biochemical assays to dissect CST complex assembly, DNA-binding specificity, and interactions with replication or repair machinery. Research on recombinant OBFC2A aids in elucidating mechanisms underlying replication stress responses and telomere homeostasis, offering potential insights into therapeutic strategies targeting telomere-related diseases or chemotherapy resistance.
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