Recombinant Human JDP2 protein

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.