Phospho-c-Jun (Thr91) Antibody #2303
- WB
Supporting Data
| REACTIVITY | H M R |
| SENSITIVITY | Endogenous |
| MW (kDa) | 48 |
| SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
Storage
Protocol
Specificity / Sensitivity
Phospho-c-Jun (Thr91) Antibody detects endogenous levels of total c-Jun protein only when phosphorylated at threonine 91. This antibody may also recognize JunB phosphorylated at Thr102.
Species Reactivity:
Human, Mouse, Rat
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.
Background
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). Knockout 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 (13). 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) (14). The identity of the protein kinase that phosphorylates Thr91 and Thr93 in vivo is unknown.
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- Leppä, S. and Bohmann, D. (1999) Oncogene 18, 6158-62.
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- Weiss, C. and Bohmann, D. (2004) Cell Cycle 3, 111-3.
- Karamouzis, M.V. et al. (2007) Mol Cancer Res 5, 109-20.
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- 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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