Product Pathways - MAPK Signaling
Phospho-c-Jun (Thr91) Antibody #2303
|W||H M R||Endogenous||48||Rabbit|
Reactivity Key: H=Human M=Mouse R=Rat
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Specificity / Sensitivity
Phospho-c-Jun (Thr91) Antibody detects endogenous levels of total c-Jun protein only when phosphorylated at threonine 91.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues around Thr91 of human c-Jun. Antibodies are purified by protein A and peptide affinity chromatography.
c-Jun is a member of the Jun family containing c-Jun, JunB, and JunD, and is a component of the transcription factor activator protein-1 (AP-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). Research studies have implicated c-Jun as a promising therapeutic target for cancer, vascular remodeling, acute inflammation, and 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.
- Jochum, W. et al. (2001) Oncogene 20, 2401-12.
- Davis, R.J. (2000) Cell 103, 239-52.
- Hilberg, F. et al. (1993) Nature 365, 179-81.
- Raivich, G. et al. (2004) Neuron 43, 57-67.
- Behrens, A. et al. (2002) EMBO J 21, 1782-90.
- Riera-Sans, L. and Behrens, A. (2007) J Immunol 178, 5690-700.
- Leppä, S. and Bohmann, D. (1999) Oncogene 18, 6158-62.
- Shaulian, E. and Karin, M. (2002) Nat Cell Biol 4, E131-6.
- Weiss, C. and Bohmann, D. (2004) Cell Cycle 3, 111-3.
- Karamouzis, M.V. et al. (2007) Mol Cancer Res 5, 109-20.
- Kim, S. and Iwao, H. (2003) J Pharmacol Sci 91, 177-81.
- Dass, C.R. and Choong, P.F. (2008) Pharmazie 63, 411-4.
- Morton, S. et al. (2003) EMBO J 22, 3876-86.
- Papavassiliou, A.G. et al. (1995) EMBO J 14, 2014-9.
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For Research Use Only. Not For Use In Diagnostic Procedures.