Technical Data
C5815-03C
c-Jun, phosphorylated, Ser63
Description:
c-Jun is a component of the transcription factor AP-1 (1). The transcriptional activity of c-Jun is regulated by phosphorylation at serines 63 and 73 (1,2). Extracellular signals, including growth factors, transforming oncoproteins and UV light, stimulate phosphorylation of c-Jun at Ser63/73 and activate c-Jun-dependent transcription (3,4).

Applications:
Suitable for use in Western Blot, Immunoprecipitation, Immunohistochemistry, Immunocytochemistry. Other applications not tested.

Recommended Dilution:
Western Blotting: 1:5,000-10,000
Immunohistochemistry: 1:50-100
Immunocytochemistry: 1:100-200
Immunoprecipitation: 1:50

Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4°C for short-term only. For long-term storage and to avoid repeated freezing and thawing, aliquot Freeze at -20°C. Aliquots are stable for at least 12 months at -20°C. 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.



Manufactured incorporating RabMAb® technology under Epitomics US patents, No 5,675,063 and 7,429,487, owned by Abcam.
TypeIsotypeCloneGrade
MabIgG6k130Supernatant
SizeStorageShippingSourceHost
100ul-20°CBlue IceHumanRabbit
Concentration:
Immunogen:
A synthetic phosphopeptide corresponding to residues surrounding Ser63 of human c-Jun
Purity:
Supernatant
Form
Supplied as a liquid
Specificity:
Recognizes human c-Jun phosphorylated at Ser63.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Bohmann, D., et al. Human proto-oncogene c-jun encodes a DNA binding protein with structural and functional properties of transcription factor AP-1. Science 238: 1386–92 (1987).
2. Smeal, T., et al. Oncogenic and transcriptional cooperation with Ha-Ras requires phosphorylation of c-Jun on serines 63 and 73. Nature 354: 494–496 (1991).
3. Derijard, B., et al. JNK1: a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain. Cell 76: 1025–1037 (1994).
4. Kyriakis, J.M., et al. The stress-activated protein kinase subfamily of c-Jun kinases. Nature 369: 156–160 (1994).