|Reactivity||Human, Mouse, Rat|
|Calculated MW||35676 Da|
|Other Names||Transcription factor AP-1, Activator protein 1, AP1, Proto-oncogene c-Jun, V-jun avian sarcoma virus 17 oncogene homolog, p39, JUN|
|Target/Specificity||A synthetic peptide corresponding to residues surrounding Threonine 91 of human c-Jun was used as an immunogen. The antibody only recognizes c-Jun phosphorylated at Threonine 91.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||c-Jun Antibody Phospho (pT91) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Transcription factor that recognizes and binds to the enhancer heptamer motif 5'-TGA[CG]TCA-3'. Promotes activity of NR5A1 when phosphorylated by HIPK3 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation. Involved in activated KRAS-mediated transcriptional activation of USP28 in colorectal cancer (CRC) cells (PubMed:24623306). Binds to the USP28 promoter in colorectal cancer (CRC) cells (PubMed:24623306).|
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Provided below are standard protocols that you may find useful for product applications.
c-Jun is a major component of the heterodimeric transcription factor AP-1 and is essential for embryonic development (1). It mediates several cellular processes, including proliferation and survival, and is upregulated in many carcinomas (2). Transactivation of c-Jun is regulated by Jun-N-terminal Kinases (JNKs) through phosphorylation at Serine 63 and 73, as well as at threonine 91 and 93 (3). Evidence supports that phosphorylation in NH2-terminal residues of c-Jun stimulates the dephosphorylation of the COOH-terminal sites, and consequently increases the DNA-binding activity of the transcription factor (4). c-Jun N-terminal kinase (JNK) isoforms are required for the phosphorylation of Threonine 91 and 93 in response to anisomycin in macrophages and TNF-alpha or anisomycin in fibroblasts (5).
1. Behrens A, et al. Nat Genet. 21(3):326-9, 1999
2. Eferl R, et al. Cell. 112(2):181-92, 2003
3. Weiss C., et al. EMBO J. 22(14): 3686-95, 2003
4. Papavassiliou, A.G., et al. EMBO J. 14(9): 2014-2019, 1995
5. Morton S., et al. The EMBO Journal 22, 3876-3886, 2003
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