CREB is a 43 kDa leucine zipper transcription factor that belongs to the CREB/ATF family. CREB regulates proliferation, differentiation and survival in diverse cell types, including cells of neuronal and hematopoietic origin. The serine 133 residue within the kinase-inducible domain (KID) is phosphorylated by various kinases. This phosphorylation promotes the interaction of CREB with various transcriptional co-activators, in particular the histone acetyltransferases CREB-binding protein (CBP) and p300. Phosphorylation of CREB occurs in response to stimuli including growth factors, neurotransmitters and stress signals that increase intracellular cAMP or calcium levels. When activated, CREB binds to cAMP response elements, thereby initiating transcription of CREB target genes. The 87G3 antibody reacts with CREB phosphorylated at the serine 133 residue.
Anti-pCREB [S133] (87G3)-165Ho—25 µg