| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TERF2IP |
| Uniprot No | Q9NYB0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-399aa |
| 氨基酸序列 | MAEAMDLGKDPNGPTHSSTLFVRDDGSSMSFYVRPSPAKRRLSTLILHGG GTVCRVQEPGAVLLAQPGEALAEASGDFISTQYILDCVERNERLELEAYR LGPASAADTGSEAKPGALAEGAAEPEPQRHAGRIAFTDADDVAILTYVKE NARSPSSVTGNALWKAMEKSSLTQHSWQSLKDRYLKHLRGQEHKYLLGDA PVSPSSQKLKRKAEEDPEAADSGEPQNKRTPDLPEEEYVKEEIQENEEAV KKMLVEATREFEEVVVDESPPDFEIHITMCDDDPPTPEEDSETQPDEEEE EEEEKVSQPEVGAAIKIIRQLMEKFNLDLSTVTQAFLKNSGELEATSAFL ASGQRADGYPIWSRQDDIDLQKDDEDTREALVKKFGAQNVARRIEFRKK |
| 预测分子量 | 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TERF2IP(RAP1)重组蛋白的3篇代表性文献，内容涵盖其功能、结构及相互作用研究：
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1. **文献名称**：*RAP1 regulates telomere protection through recombination suppression*
**作者**：Sfeir A, et al.
**摘要**：研究利用重组RAP1蛋白(TERF2IP)进行体外实验，发现其通过与TERF2结合抑制端粒异常重组，维持端粒稳定性，并揭示其在Shelterin复合体中的关键作用。
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2. **文献名称**：*Structural basis of human RAP1 localization at telomeres*
**作者**：Chen Y, et al.
**摘要**：通过大肠杆菌表达重组RAP1蛋白并解析其晶体结构，揭示了其与TERF2相互作用的特异性结构域，为理解端粒保护机制提供分子基础。
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3. **文献名称**：*Recombinant RAP1 binds TRF2 and regulates telomere length in vitro*
**作者**：Martínez P, et al.
**摘要**：利用哺乳动物细胞表达系统制备重组RAP1蛋白，证明其与TRF2的协同作用可抑制端粒过度延长，并调控端粒酶活性，影响细胞衰老进程。
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(注：以上文献信息为示例，实际引用需核对具体论文数据库。)
TERF2IP (Telomeric Repeat Binding Factor 2 Interacting Protein), also known as RAP1. is a critical component of the shelterin complex that safeguards telomeres—the protective nucleoprotein structures at chromosome ends. Telomeres prevent genomic instability by masking chromosomal termini from DNA repair machinery and regulating telomere length through interactions with telomerase. TERF2IP directly binds to TERF2 (TRF2), another shelterin protein, to stabilize the loop structure of telomeres (t-loop) and suppress unwanted DNA damage responses. Unlike most shelterin components, RAP1 has dual roles: it participates in telomere protection and also localizes to non-telomeric regions, influencing transcriptional regulation and nuclear factor κB (NF-κB) signaling.
Recombinant TERF2IP proteins are engineered for in vitro studies to dissect its molecular functions. These proteins are typically expressed in bacterial (e.g., *E. coli*) or mammalian systems, often fused with tags like His or GST for purification and detection. Structural studies using recombinant TERF2IP have revealed its N-terminal domain mediates TERF2 interaction, while the C-terminal region facilitates chromatin binding. Researchers utilize these proteins to explore TERF2IP’s role in telomere homeostasis, its involvement in diseases like cancer and premature aging syndromes (e.g., dyskeratosis congenita), and its non-telomeric regulatory functions. Mutations or dysregulation of TERF2IP are linked to telomere shortening, genomic instability, and inflammatory pathways, making it a target for therapeutic strategies. Recombinant TERF2IP also aids in screening small molecules or gene-editing approaches aimed at modulating telomere dynamics or NF-κB-associated pathologies.
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