Product Pathways - Motif Antibodies
PTMScan® Acetyl-Lys Motif (Ac-K) Immunoaffinity Beads
|Consenus Site||Cell or Tissue Type||Study No.||Modified Peptides Identified|
|Ac-K||Jurkat (T cell acute lymphoblastic leukemia)||2292||283|
This product is not for individual sale. It is only available as a component of the PTMScan® Proteomics System. PTMScan® Proteomics System orders must be priced out individually. Please email us at firstname.lastname@example.org to receive the most accurate pricing.
PTMScan® Immunoaffinity Beads are custom preparations of motif antibodies coupled to protein A beads. They are intended only for use for PTMScan® and are available as components of the PTMScan® Proteomics System.
Specificity / Sensitivity
PTMScan® Acetyl-Lys Motif (Ac-K) Immunoaffinity Beads detect and capture endogenous levels of peptide derived from protease digested cellular proteins modified by acetylation on the epsilon-amine groups of lysine residues. The antibody recognizes acetylated lysine in a wide range of sequence contexts. (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.)
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.
Have you published research involving the use of our products? If so we'd love to hear about it. Please let us know!
For Research Use Only. Not For Use In Diagnostic Procedures.