After the primary antibody is bound to the target protein, a complex with HRP-linked secondary antibody is formed. The LumiGLO® is added and emits light during enzyme catalyzed decomposition.
Phospho-ATF-2 (Thr71) Antibody detects endogenous levels of ATF-2 only when phosphorylated at Thr71. It recognizes this site regardless of the phosphorylation state of Thr69. ATF-2 (20F1) Rabbit mAb detects endogenous levels of total ATF-2 protein. Neither antibody cross-reacts with c-Jun, CREB or other transcription factors.
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Thr71 of human ATF-2 (Phospho-ATF-2 (Thr71) Antibody), or with a synthetic peptide corresponding to the amino terminal sequence of human ATF-2 (ATF-2 (20F1) Rabbit mAb). Antibodies are purified by protein A and peptide affinity chromatography.
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).
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