Phospho-c-Jun (Thr93) Antibody detects endogenous levels of c-Jun only when phosphorylated at threonine 93.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues around Thr93 of human c-Jun. Antibodies are purified by protein A and peptide affinity chromatography.
Background
c-Jun is a member of the Jun Family containing c-Jun, JunB and JunD, and is a component of the transcription factor AP-1 (activator protein-1). AP-1 is composed of dimers of Fos, Jun and ATF family members and binds to and activates transcription at TRE/AP-1 elements (reviewed in 1). Extracellular signals including growth factors, chemokines and stress activate AP-1-dependent transcription. The transcriptional activity of c-Jun is regulated by phosphorylation at Ser63 and Ser73 through SAPK/JNK (reviewed in 2). Knock-out studies in mice have shown that c-Jun is essential for embryogenesis (3), and subsequent studies have demonstrated roles for c-Jun in various tissues and developmental processes including axon regeneration (4), liver regeneration (5) and T cell development (6). AP-1 regulated genes exert diverse biological functions including cell proliferation, differentiation, and apoptosis, as well as transformation, invasion and metastasis, depending on cell type and context (7-9). Other target genes regulate survival as well as hypoxia and angiogenesis (8,10). c-Jun has emerged as a promising therapeutic target for cancer, vascular remodeling, acute inflammation, as well as rheumatoid arthritis (11,12).The multisite phosphorylation of the transcription factor c-Jun has been reinvestigated recently (14). The phosphorylation of Thr91 and Thr93 induces a change in the conformation of c-Jun that enhances accessibility of the carboxy-terminal sites to a protein phosphatase(s) (15). The identity of the protein kinase that phosphorylates Thr91 and Thr93 in vivo is unknown.