Technical Data
c-Jun, phosphorylated (Ser73)
c-Jun is a component of the transcription factor AP-1, which binds and activates transcription at TRE/AP-1 elements. The transcriptional activity of c-Jun is regulated by phosphorylation at Ser63 and Ser73 (1,2). Extracellular signals, including growth factors, transforming oncoproteins and UV irradiation, stimulate phosphorylation of c-Jun at Ser63/73 and activate c-Jun-dependent transcription. Mutation of Ser63/73 renders c-Jun nonresponsive to mitogenic and stressinduced signaling pathways. The MAP kinase homologue SAPK/JNK binds to the N-terminal region of c-Jun and phosphorylates c-Jun at Ser63/73. In addition, the activity of SAPK/JNK is stimulated by the same signals that activate c-Jun (3,4).

Suitable for use in ELISA, Western Blot and Immunofluorescence. Other applications not tested.

Recommended Dilution:
Western Blot: 1:1000
Immunofluorescence (IF-IC): 1:100
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. For long-term storage, store at -20C. Aliquots are stable for at least 12 months at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
PabIgGAffinity Purified
100ul4C (-20C Glycerol)Blue IceHumanRabbit
Not determined
Synthetic phosphopeptide (KLH coupled) corresponding to residues around Ser73 of human c-Jun.
Purified by Protein A and immunoaffinity chromatography.
Supplied as liquid in 10mM HEPES, pH 7.5, 150mM sodium chloride, 0.1mg/ml BSA, 50% glycerol. No preservative added.
Detects endogenous levels of c-Jun only when activated by phosphorylation at Ser73. Also recognizes phosphorylation of JunD at Ser100. Species Crossreactivity: Human, mouse and rat.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Binetruy, B., et al., (1991) Nature 351: 122-127. 2. Smeal, T., et al., (1991) Nature 354: 494-496. 3. Derijard, B., et al., (1994) Cell 76: 1,025-1,037. 4. Kyriakis, J.M., et al., (1994) Nature 369: 156-160. 5. de Ruiter, N.D., et al., (2000) Mol. Cell. Biol. 20: 8,480-8,488. 6. Fan, M., et al., (2000) J. Biol. Chem. 275: 29,980-29,985. 7. Lee, S.A., et al., (2001) J. Biol. Chem. 276: 11,783-11,790. 8. Paasinen-Sohns, A., et al., (2000) J. Cell Biol. 151: 801-810.