Render Target: STATIC
Render Timestamp: 2024-12-23T12:11:42.479Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-09-30 01:54:20.072
Product last modified at: 2024-12-17T18:49:14.803Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

Malonyl-Lysine [Mal-K] MultiMab® Rabbit mAb mix #14942

Filter:
  • WB

    Supporting Data

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

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000

    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

    Malonyl-Lysine [Mal-K] MultiMab® Rabbit mAb mix recognizes endogenous levels of proteins only when malonylated at a lysine residue. This antibody does not cross-react with other lysine modifications.

    Species Reactivity:

    All Species Expected

    Source / Purification

    MultiMab® Rabbit mAb mixes are prepared by combining individual rabbit monoclonal clones in optimized ratios for the approved applications. Each antibody in the mix is carefully selected based on motif recognition and performance in multiple assays. Each mix is engineered to yield the broadest possible coverage of the modification being studied while ensuring a high degree of specificity for the modification or motif.

    Background

    Lysine is subject to a wide array of regulatory post-translational modifications due to its positively charged ε-amino group side chain. The most prevalent of these are ubiquitination and acetylation, which are highly conserved among prokaryotes and eukaryotes (1,2). Acyl group transfer from the metabolic intermediates acetyl-, succinyl-, malonyl-, glutaryl-, butyryl-, propionyl-, and crotonyl-CoA all neutralize lysine’s positive charge and confer structural alterations affecting substrate protein function. Lysine acetylation is catalyzed by histone acetyltransferases, HATs, using acetyl-CoA as a cofactor (3,4). Deacylation is mediated by histone deacetylases, HDACs 1-11, and NAD-dependent Sirtuins 1-7. Some sirtuins have little to no deacetylase activity, suggesting that they are better suited for other acyl lysine substrates (5).
    SIRT5 is a predominantly mitochondrial desuccinylase and demalonylase (5,6). In the absence of a known malonyltransferase, nonenzymatic protein malonylation is likely driven by the concentration of malonyl-CoA and intracellular pH and is subject to metabolic fluctuations (7). Malonylation is especially prevalent among mitochondrial metabolic proteins. In type II diabetes mouse models, notably elevated malonylation can be detected mainly, but not exclusively, on proteins of glucose and fatty acid metabolism (8). Yeast histone H3K56 malonylation suggests poor DNA binding efficiency and may lead to reduced cell viability (9).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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