Recombinant Human JUN protein

The JUN recombinant protein is derived from the c-Jun proto-oncogene, a key component of the activator protein-1 (AP-1) transcription factor family. c-Jun, first identified as a viral oncogene homolog (v-Jun), plays a central role in regulating gene expression linked to cell proliferation, differentiation, apoptosis, and stress responses. Structurally, JUN contains a basic leucine zipper (bZIP) domain that facilitates dimerization with other AP-1 members (e.g., FOS, ATF) and binds to specific DNA sequences (TRE/CRE motifs) to modulate transcriptional activity. Its function is tightly regulated by post-translational modifications, such as phosphorylation by kinases like JNK (c-Jun N-terminal kinase), which activates AP-1-dependent gene programs in response to cytokines, growth factors, or cellular stressors.

Recombinant JUN proteins are typically produced using expression systems like *E. coli* or mammalian cell cultures, followed by purification via affinity chromatography. These engineered proteins retain functional domains critical for studying AP-1 signaling mechanisms, including dimerization, DNA binding, and interactions with co-regulators. Researchers employ JUN recombinant proteins in diverse applications: dissecting MAPK/AP-1 pathway dynamics, modeling diseases (e.g., cancer, inflammation), and screening compounds that modulate AP-1 activity for therapeutic development. Additionally, structural studies using recombinant JUN have advanced understanding of its interaction interfaces, aiding drug design targeting aberrant AP-1 activity in oncology and autoimmune disorders. As a versatile tool, JUN recombinant protein bridges molecular biology and translational research, offering insights into cellular decision-making and therapeutic targeting of AP-1-driven pathologies.