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ATF-2 is part of the ATF/CREB family consists of sixteen cellular stress-responsive transcription factors. The common feature of all ATF proteins is the bZIP element, formed by a leucine zipper subdomain and a basic region subdomain, through which they can both dimerize and bind to specific DNA sequences. In unstimulated cells, ATF-2 is maintained in a transcriptionally inactive form by intramolecular interactions between its own activation domain and its bZIP domain. After stimulation, ATF-2 is phosphorylated by JNK on Thr69 and Thr71 and form homo- or heterodimers that bind to specific DNA sequences on target gene promoters. ATF-2 dimers bind preferentially to the 8-base palindromic CRE (cAMP Responsive Element) consensus sequence but also the AP-1 element, the proximal element of IFN-gamma promoter the stress-response element (StRE) of ho-1 gene and the UV-Responsive Element (URE). ATF-2 binding to DNA activates a variety of gene targets including cyclin A, cyclin D and c-jun. The ATF-2 is manufactured as a maltose binding protein (MBP) fusion protein with an amino terminal polyhistidine tag.