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.
Buffer
Store at -20C. Buffer: 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA. Stable for 12 months from date of receipt.
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).
Related Pathway
Apoptosis
Delta-Notch Signaling Pathway
EGFR1 Signaling Pathway
Focal Adhesion
MAPK signaling pathway
TGF Beta Signaling Pathway
Toll-like receptor signaling pathway
Wnt Signaling Pathway
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