| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | JDP2 |
| Uniprot No | Q8WYK2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-163aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMMPGQI PDPSVTTGSL PGLGPLTGLP SSALTVEELK YADIRNLGAM IAPLHFLEVK LGKRPQPVKS ELDEEEERRK RRREKNKVAA ARCRNKKKER TEFLQRESER LELMNAELKT QIEELKQERQ QLILMLNRHR PTCIVRTDSV KTPESEGNPL LEQLEKK |
| 预测分子量 | 21 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JDP2重组蛋白的3篇示例参考文献(注：文献信息为模拟示例，非真实存在)：
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1. **文献名称**：*"Expression and Functional Analysis of Recombinant JDP2 in DNA Binding Assays"*
**作者**：Smith A. et al.
**摘要**：本研究利用大肠杆菌表达系统成功克隆并纯化了重组JDP2蛋白，通过电泳迁移率实验(EMSA)证实其特异性结合AP-1位点DNA的能力，为研究JDP2在转录调控中的作用提供了工具。
2. **文献名称**：*"JDP2 Recombinant Protein Modulates Oxidative Stress Response in Cellular Models"*
**作者**：Zhang Y. et al.
**摘要**：通过昆虫细胞表达系统制备高纯度JDP2重组蛋白，发现其通过抑制Nrf2通路降低细胞氧化应激损伤，揭示了JDP2在抗氧化机制中的潜在应用价值。
3. **文献名称**：*"Structural Characterization of JDP2 Recombinant Protein Using X-ray Crystallography"*
**作者**：Tanaka K. et al.
**摘要**：首次解析了重组JDP2蛋白的晶体结构，明确了其与c-Jun结合的关键结构域，为设计靶向JDP2的小分子抑制剂提供了结构基础。
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如需真实文献，建议在PubMed或Google Scholar中检索关键词：**JDP2 recombinant protein expression**、**JDP2 purification** 或 **JDP2 functional study**。
JDP2 (Jun Dimerization Protein 2) is a member of the AP-1 transcription factor family, which plays a critical role in regulating gene expression involved in cellular processes such as proliferation, differentiation, apoptosis, and stress responses. Originally identified as a binding partner for c-Jun, JDP2 forms dimers with Jun/Fos family proteins to modulate their transcriptional activity. It contains a basic leucine zipper (bZIP) domain that mediates DNA binding and protein-protein interactions. Unlike some AP-1 members, JDP2 exhibits dual functionality, acting as both a transcriptional repressor and activator, depending on cellular context and binding partners.
JDP2 has been implicated in diverse biological pathways, including cell cycle regulation, oxidative stress responses, and chromatin remodeling. Studies highlight its role in cancer, where it may act as a tumor suppressor or promoter, depending on the cancer type. For example, JDP2 suppresses tumor growth in certain models by inhibiting AP-1-driven oncogenesis, while in others, it promotes metastasis via epithelial-mesenchymal transition (EMT). Its involvement in inflammatory diseases and fibrosis has also been explored, linking JDP2 to pathways like TGF-β signaling.
Recombinant JDP2 protein is typically produced using bacterial (e.g., E. coli) or mammalian expression systems, enabling in vitro studies of its structure, DNA-binding properties, and interactions with other transcriptional regulators. Purified JDP2 is utilized to investigate its mechanistic roles, screen for small-molecule inhibitors, or develop therapeutic strategies targeting AP-1-associated pathologies. Structural analyses of recombinant JDP2 have provided insights into its dimerization specificity and DNA-binding motifs, aiding the design of synthetic regulators. Ongoing research aims to clarify its context-dependent functions and therapeutic potential in diseases characterized by aberrant AP-1 activity.
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