Acetylated-Lysine (Ac-K2-100) MultiMab® Rabbit mAb mix #9814
- WB
- IP
- ChIP
Supporting Data
| REACTIVITY | All |
| SENSITIVITY | Endogenous |
| MW (kDa) | |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
- ChIP-Chromatin Immunoprecipitation
Species Cross-Reactivity Key:
- All-All Species Expected
Product Information
Product Usage Information
For optimal ChIP results, use 10 μl of antibody and 10 μg of chromatin (approximately 4 x 106 cells) per IP. This antibody has been validated using SimpleChIP® Enzymatic Chromatin IP Kits.
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:100 |
| Chromatin IP | 1:50 |
| Peptide ELISA (DELFIA) | 1:1000 |
Storage
Protocol
Specificity / Sensitivity
Acetylated-Lysine (Ac-K-100) MultiMab® Rabbit mAb mix recognizes proteins post-translationally modified by acetylation on the ε-amine groups of lysine residues. The antibody recognizes acetylated lysine in a wide range of sequence contexts. It has been demonstrated to recognize acetylated histones, p53, CBP, PCAF and chemically acetylated BSA. The antibody has been shown to react with as little as 0.04 ng of chemically acetylated BSA while not recognizing up to 25 µg of non-acetylated BSA.
Species Reactivity:
All Species Expected
Source / Purification
MultiMab® rabbit monoclonal mix antibodies are prepared by combining individual rabbit monoclonal clones in optimized ratios for the approved applications. Each antibody in the mix is carefully selected based on motif recognition and performance in multiple assays. Each mix is engineered to yield the broadest possible coverage of the modification being studied while ensuring a high degree of specificity for the modification or motif.
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.
Limited Uses
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