Render Target: STATIC
Render Timestamp: 2024-09-26T09:45:25.890Z
Commit: 60a5021c3a47fc24d1656fb463e2c3c41a1ad145
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

Acetylated-Lysine Antibody #9441

Filter:
  • WB
  • IP
  • IHC
  • IF
  • ChIP

    Supporting Data

    REACTIVITY All
    SENSITIVITY Endogenous
    MW (kDa)
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    • IHC-Immunohistochemistry 
    • IF-Immunofluorescence 
    • ChIP-Chromatin Immunoprecipitation 
    Species Cross-Reactivity Key:
    • All-All Species Expected 

    Product Information

    Product Usage Information

    For optimal ChIP results, use 10 μl of antibody and 10 μg of chromatin (approximately 4 x 106 cells) per IP. This antibody has been validated using SimpleChIP® Enzymatic Chromatin IP Kits.

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:100
    Immunohistochemistry (Paraffin) 1:300 - 1:1200
    Immunofluorescence (Immunocytochemistry) 1:100 - 1:400
    Chromatin IP 1:25
    Peptide ELISA (DELFIA) 1:2000

    Storage

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

    Protocol

    Specificity / Sensitivity

    Acetylated-Lysine Antibody detects proteins posttranslationally modified by acetylation on the epsilon-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 nonacetylated BSA.

    Species Reactivity:

    All Species Expected

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic acetylated lysine-containing peptide. Antibodies are purified by protein A and peptide affinity chromatography.

    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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