Product Pathways - Motif Antibodies
Acetylated-Lysine Mouse mAb (Ac-K-103) #9681
|W E-P||All||Endogenous||Mouse IgG2a|
Reactivity Key: All=All species expected
Species cross-reactivity is determined by western blot.
Specificity / Sensitivity
Acetylated-Lysine Mouse mAb (Ac-K-103) detects proteins only when posttranslationally modified by acetylation on the epsilon-amine groups of lysine residues. Detection of acetylated lysine by this antibody is largely independent of surrounding amino acid sequence. The antibody has been shown to recognize acetylated proteins including histones, p53, CBP, PCAF and chemically acetylated BSA. (U.S. Patent No's.: 6,441,140; 6,982,318; 7,259,022; 7,344,714; U.S.S.N. 11,484,485; and all foreign equivalents.)
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic acetylated lysine-containing peptide.
Western blot analysis of extracts from COS cells, untreated or TSA-treated (0.4 µM for 18 hours), using Acetylated-Lysine Mouse mAb (Ac-K-103).
Acetylation of lysine, like phosphorylation of serine, threonine or tyrosine, is an important reversible modification controlling protein activity. The conserved amino-terminal domains of the four core histones (H2A, H2B, H3, and H4) contain lysines that are acetylated by histone acetyltransferases (HATs) and deacetylated by histone deacetylases (HDACs) (1). Signaling resulting in acetylation/deacetylation of histones, transcription factors, and other proteins affects a diverse array of cellular processes including chromatin structure and gene activity, cell growth, differentiation, and apoptosis (2-6). Recent proteomic surveys suggest that acetylation of lysine residues may be a widespread and important form of posttranslational protein modification that affects thousands of proteins involved in control of cell cycle and metabolism, longevity, actin polymerization, and nuclear transport (7,8). The regulation of protein acetylation status is impaired in cancer and polyglutamine diseases (9), and HDACs have become promising targets for anti-cancer drugs currently in development (10).
- Hassig, C.A. and Schreiber, S.L. (1997) Curr Opin Chem Biol 1, 300-8.
- Allfrey, V.G. et al. (1964) Proc Natl Acad Sci USA 51, 786-94.
- Liu, L. et al. (1999) Mol Cell Biol 19, 1202-9.
- Boyes, J. et al. (1998) Nature 396, 594-8.
- Polevoda, B. and Sherman, F. (2002) Genome Biol 3, reviews0006.
- Yoshida, M. et al. (2003) Prog Cell Cycle Res 5, 269-78.
- Kim, S.C. et al. (2006) Mol Cell 23, 607-18.
- Choudhary, C. et al. (2009) Science 325, 834-40.
- Hughes, R.E. (2002) Curr Biol 12, R141-3.
- Vigushin, D.M. and Coombes, R.C. (2004) Curr Cancer Drug Targets 4, 205-18.
- Czuwara-Ladykowska, J. et al. (2002) J Biol Chem 277, 20399-408. Applications: Western Blotting
- Deng, W.G. and Wu, K.K. (2003) J Immunol 171, 6581-8. Applications: Western Blotting
- Chang, C.W. et al. (2005) Mol Cell Biol 25, 8401-14. Applications: Western Blotting
- Chuang, H.C. et al. (2006) Nucleic Acids Res 34, 1459-69. Applications: Western Blotting
- Zhao, L.J. et al. (2006) J Biol Chem 281, 36613-23. Applications: Western Blotting
- Yang, S.R. et al. (2007) Am J Physiol Lung Cell Mol Physiol 292, L567-76. Applications: Western Blotting
- VanDemark, A.P. et al. (2007) Mol Cell 27, 817-28. Applications: Western Blotting
Have you published research involving the use of our products? If so we'd love to hear about it. Please let us know!
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License/Use Restrictions: Use of CST Motif Antibodies within certain methods (e.g., U.S. Patent No.'s 7,198,896 & 7,300,753) may require a license from CST. For information regarding academic licensing terms please have your technology transfer office contact CST Legal Department at CST_ip@cellsignal.com. For information regarding commercial licensing terms please contact CST Pharma Services Department at firstname.lastname@example.org.
For Research Use Only. Not For Use In Diagnostic Procedures.