Description
Product Usage Information
This formulation is ideal for use with technologies requiring specialized or custom antibody labeling, including fluorophores, metals, lanthanides, and oligonucleotides. It is not recommended for ChIP, ChIP-seq, CUT&RUN or CUT&Tag assays. If you require a carrier free formulation for chromatin profiling, please contact us . Optimal dilutions/concentrations should be determined by the end user. BSA and Azide Free antibodies are quality control tested by size exclusion chromatography (SEC) to determine antibody integrity.
Formulation
Supplied in 1X PBS (10 mM Na 2 HPO 4 , 3 mM KCl, 2 mM KH 2 PO 4 , and 140 mM NaCl (pH 7.8)). BSA and Azide Free.
Storage
Store at -20°C. This product will freeze at -20°C so it is recommended to aliquot into single-use vials to avoid multiple freeze/thaw cycles. A slight precipitate may be present and can be dissolved by gently vortexing. This will not interfere with antibody performance.
Specificity / Sensitivity
Acetylated-Lysine (A3D6C) Rabbit Monoclonal Antibody (BSA and Azide Free) detects proteins only when posttranslationally modified by acetylation on the epsilon-amine groups of lysine residues. This antibody recognizes acetylated lysine in a wide range of sequence contexts.
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).
