Main Information

Target

Acetyl Lys proteins

Host Species

Rabbit

Reactivity

Human, Mouse, Rat, Monkey, plant

Applications

WB, IHC, IF, ELISA

MW

20,40,80,175kD (Observed)

Conjugate/Modification

Acetyl

Detailed Information

Recommended Dilution Ratio

WB 1:500-1:2000; IHC 1:100-1:300; IF 1:200-1:1000; ELISA 1:10000; Not yet tested in other applications.

Formulation

Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.

Specificity

Acetyl-Lys proteins Polyclonal Antibody detects endogenous levels of acetylated Lys proteins.

Purification

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.

Storage

-15°C to -25°C/1 year(Do not lower than -25°C)

Concentration

1 mg/ml

MW(Observed)

20,40,80,175kD

Modification

Acetyl

Clonality

Polyclonal

Isotype

IgG

Antigen&Target Information

Immunogen:

Synthesized acetyl-peptide derived from human acetylation Lys proteins.

Specificity:

Acetyl-Lys proteins Polyclonal Antibody detects endogenous levels of acetylated Lys proteins.

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). 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. 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. The regulation of protein acetylation status is impaired in cancer and polyglutamine diseases, and HDACs have become promising targets for anti-cancer drugs currently in development.