Mouse anti-All Lysine Monoclonal Antibody

Acetyl Lysine Monoclonal Antibody

Cat. Num. AAA9700442

• Reactivity: All
• Applications: Western Blot, Immunohistochemistry
• Purity: Affinity-purified from mouse ascites by affinity-chromatography using epitope-specific immunogen.
• Synonyms: Lysine; Monoclonal Antibody; Acetyl Lysine Monoclonal Antibody; Mouse Anti-Acetyl Lysine Monoclonal Antibody; anti-Lysine antibody

• Host: Mouse
• Reactivity: All
• Clonality: Monoclonal
• Isotype: IgG1
• Specificity: The antibody detects endogenous Acetyl Lysine protein.
• Purity/Purification: Affinity-purified from mouse ascites by affinity-chromatography using epitope-specific immunogen.
• Form/Format: Liquid; PBS, pH 7.4, Containing 0.02% Sodium Azide As Preservative and 50% Glycerol.
• Concentration: 1 mg/ml (varies by lot)

• Applicable Applications for anti-Lysine antibody: Western Blot (WB), Immunohistochemistry (IHC) Paraffin
• Application Notes: WB: 1:1000-1:2000; IHC-P: 1:200-1:500
• Immunogen: Purified Protein
• Preparation and Storage: Stable for one year at -20 degree C from date of shipment.; For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Aliquot to avoid repeated freezing and thawing.

Western Blot (WB)

(Fig.1. Western blot analysis of 1) Mouse Brain Tissue, 2) Hela, 3) Hela+TSA Treated using Acetyl Lysine Monoclonal Antibody.)

Immunohistochemistry (IHC)

(Fig.2. Immunohistochemical analysis of paraffin-embedded Human Breast Carcinoma using Acetyl Lysine Monoclonal Antibody.)

Related Product Information for anti-Lysine antibody

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.