JunD Rabbit Recombinant mAb detects endogenous levels of total JunD.

JunD, a basic region leucine zipper DNA-binding protein, is a member of the Jun family of proteins that are primary components of the activating protein-1 (AP-1) transcription factor. Jun proteins can form AP-1 homodimers or heterodimers among themselves or with members of the related Fos or activating factor/cAMP response element binding protein families, and directly bind to their target promoters at specific DNA elements. All three Jun proteins (c-Jun, JunB, and JunD) are similar in DNA-binding affinity, but their expression patterns vary in response to stress and during cell proliferation and transformation. c-Jun and JunB behave as immediate-early response genes and enhance the G1-to-S-phase transition upon mitogenic stimulation, while JunD can inhibit cell proliferation. JunD also regulates apoptosis and protects against oxidative stress by modulating genes involved in the antioxidant defense and hydrogen peroxide production. JunD contains an acceptor Serine and can be phosphorylated by JNK in c-Jun/JunD heterodimers. In contrast with c-jun and junB, junD is relatively refractory to serum stimulation and its basal expression remains high in many cell types.