Acetylated-Lysine (Ac-K-103) Mouse mAb #9681
Filter:
- WB
Supporting Data
| REACTIVITY | All |
| SENSITIVITY | Endogenous |
| MW (kDa) | |
| Source/Isotype | Mouse IgG2a |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- All-All Species Expected
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Peptide ELISA (DELFIA) | 1:1000 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
Acetylated-Lysine (Ac-K-103) Mouse mAb 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.)
Species Reactivity:
All Species Expected
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic acetylated lysine-containing peptide.
Background
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 post-translational 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, reviews 0006.
- 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.
限制使用
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For Research Use Only. Not For Use In Diagnostic Procedures.
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