Phospho-ATF2 (Thr71) (G3) rabbit mAb FITC conjugate

Activating transcription factor 2 (ATF2), known as cyclic AMP (cAMP) response element (CRE) binding protein 2 (CREB2) and CRE-BP1 is a member of the activating protein-1 (AP1) transcription factor family. Through homo-dimerization or hetero-dimerization with other AP1 family members, such as the CREB, Fos, Maf, or Jun family transcription factor, it regulates the expression of many genes. ATF2 is an important mediator of mammalian cell responses to various stimuli, including stress. As a transcription factor, ATF2 acts as transducing extracellular signals to the nucleus to facilitate transcriptional responses to stimuli. ATF2 is stimulated by growth factors, ultraviolet (UV) radiation, and cytokines. Stress-activated protein kinases (SAPKs)(e.g. p38 MAP Kinase) induce transcriptional activation of ATF2. ATF2 is phosphorylated at amino acids threonine-69 and threonine-71 (T69, T71). Phosphorylation at these threonine residues is essential for maximal transcriptional activity downstream of insulin/epidermal growth factor stimulation and is dependent on cooperation between c-Jun N-terminal kinase (JNK) and signaling cascades downstream of Ras. Upon T69/T71 phosphorylation, ATF2 interacts with other AP1 proteins and translocate to the nucleus to regulate the expression of hundreds of genes.