Cell Signaling Technology

Product Pathways - Motif Antibodies

Acetylated-Lysine (Ac-K2-100) Rabbit mAb (HRP Conjugate) #6952

Applications Reactivity Sensitivity Isotype
W All Endogenous Rabbit IgG

Applications Key:  W=Western Blotting
Reactivity Key: All=All species expected
Species cross-reactivity is determined by western blot.

Protocols

Specificity / Sensitivity

Acetylated-Lysine (Ac-K2-100) Rabbit mAb (HRP Conjugate) detects 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. (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 acetyl-lysine peptide library. The antibody is formulated from two rabbit monoclones in order to cover broad range of reactivity.

Western Blotting

Western Blotting

Western blot analysis of extracts from MCF7 cells, untreated or treated with Trichostatin A (TSA) #9950 (1 µM, 6 hr), using Acetylated-Lysine (Ac-K2-100) Rabbit mAb (HRP Conjugate).

ELISA-Peptide

ELISA-Peptide

Signal-to-noise (S/N) values of acetylated versus non-acetylated peptides analyzed using Acetylated-Lysine (Ac-K2-100) Rabbit mAb (HRP Conjugate) and 20X LumiGLO® Reagent and 20X Peroxide #7003.

Description

This Cell Signaling Technology® antibody is conjugated by the covalent reaction of hydrazinonicotinamide-modified antibody with formylbenzamide-modified horseradish peroxidase (HRP). The HRP conjugated antibody is expected to exhibit the same species cross-reactivity as the unconjugated Acetylated-Lysine (Ac-K2-100) Rabbit mAb #9814.

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 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).

  1. Hassig, C.A. and Schreiber, S.L. (1997) Curr Opin Chem Biol 1, 300-8.
  2. Allfrey, V.G. et al. (1964) Proc Natl Acad Sci USA 51, 786-94.
  3. Liu, L. et al. (1999) Mol Cell Biol 19, 1202-9.
  4. Boyes, J. et al. (1998) Nature 396, 594-8.
  5. Polevoda, B. and Sherman, F. (2002) Genome Biol 3, reviews0006.
  6. Yoshida, M. et al. (2003) Prog Cell Cycle Res 5, 269-78.
  7. Kim, S.C. et al. (2006) Mol Cell 23, 607-18.
  8. Choudhary, C. et al. (2009) Science 325, 834-40.
  9. Hughes, R.E. (2002) Curr Biol 12, R141-3.
  10. Vigushin, D.M. and Coombes, R.C. (2004) Curr Cancer Drug Targets 4, 205-18.

Application References

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Companion Products

For Research Use Only. Not For Use In Diagnostic Procedures.

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