Render Target: STATIC
Render Timestamp: 2024-12-27T11:44:33.448Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-09-30 01:57:11.381
Product last modified at: 2024-12-17T19:05:11.734Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77

Acetylated-Lysine (Ac-K-103) Mouse mAb #9681

Filter:
  • WB

    Supporting Data

    REACTIVITY All
    SENSITIVITY Endogenous
    MW (kDa)
    Source/Isotype Mouse IgG2a
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • All-All Species Expected 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Peptide ELISA (DELFIA) 1:1000

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    Acetylated-Lysine (Ac-K-103) Mouse mAb detects proteins only when posttranslationally modified by acetylation on the epsilon-amine groups of lysine residues. Detection of acetylated lysine by this antibody is largely independent of surrounding amino acid sequence. The antibody has been shown to recognize acetylated proteins including histones, p53, CBP, PCAF and chemically 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.)

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