Phospho-ATF-2 (Thr69)/ATF-7 (Thr51) (E3D6B) Rabbit mAb detects endogenous levels of ATF-2 and ATF-7 only when phosphorylated at Thr69 and Thr51, respectively. It recognizes Thr69/Thr71 dually phosphorylated ATF-2, Thr51/Thr53 dually phosphorylated ATF-7, Thr69 singly phosphorylated ATF-2, and Thr51 singly phosphorylated ATF-7 equally well but does not detect singly phosphorylated Thr71 of ATF-2 and singly phosphorylated Thr53 of ATF-7.

Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Thr69 and Thr71 of human ATF-2 protein.

The transcription factor ATF-2 (also called CRE-BP1) binds to both AP-1 and CRE DNA response elements and is a member of the ATF/CREB family of leucine zipper proteins (1). ATF-2 interacts with a variety of viral oncoproteins and cellular tumor suppressors and is a target of the SAPK/JNK and p38 MAP kinase signaling pathways (2-4). Various forms of cellular stress, including genotoxic agents, inflammatory cytokines, and UV irradiation, stimulate the transcriptional activity of ATF-2. Cellular stress activates ATF-2 by phosphorylation of Thr69 and Thr71 (2-4). Both SAPK and p38 MAPK have been shown to phosphorylate ATF-2 at these sites in vitro and in cells transfected with ATF-2. Mutations of these sites result in the loss of stress-induced transcription by ATF-2 (2-4). In addition, mutations at these sites reduce the ability of E1A and Rb to stimulate gene expression via ATF-2 (2).
ATF-7 is another member of the ATF/CREB family of leucine zipper proteins (5). Similarly, Thr51 and Thr53 (corresponding to Thr69 and Thr71 of ATF-2, respectively) can be phosphorylated under different conditions (6,7).