Render Target: STATIC
Render Timestamp: 2024-11-21T13:34:54.168Z
Commit: 5c4accf06eb7154018ba3f54329c7590f97f534a
XML generation date: 2024-04-24 09:09:09.782
Product last modified at: 2024-11-13T22:30:11.118Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77

O-GlcNAc (CTD110.6) Mouse mAb (HRP Conjugate) #12938

Filter:
  • WB

    Supporting Data

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

    Product Information

    Product Description

    This Cell Signaling Technology® antibody is conjugated to the carbohydrate groups of horseradish peroxidase (HRP) via its amine groups. The HRP conjugated antibody is expected to exhibit the same species cross-reactivity as the unconjugated O-GlcNAc (CTD110.6) Mouse mAb #9875.

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000

    Storage

    Supplied in 136 mM NaCl, 2.6 mM KCI, 12 mM sodium phosphate (pH 7.4) dibasic, 2 mg/ml BSA, and 50% glycerol. Store at –20°C. Do not aliquot the antibodies.

    Protocol

    Specificity / Sensitivity

    O-GlcNAc (CTD110.6) Mouse mAb (HRP Conjugate) specifically recognizes endogenous levels of O-GlcNAc on proteins in β-O-glycosidic linkage to both serine and threonine.

    Species Reactivity:

    All Species Expected

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a peptide containing serine-O-linked N-acetylglucosamine (O-GlcNAc).

    Background

    A distinct form of protein glycosylation, beta-linked N-acetyl-glucosamine (GlcNAc) moieties can be added to serine or threonine residues of proteins (1,2). This differs from other forms of glycosylation, as it typically is a single moiety rather than the complex branched sugars that are more commonly studied. It is thought that these modifications happen in a much more dynamic cycle more reminiscent of phosphorylation modifications. GlcNAc modified proteins are found in the cytoplasm and nucleus and are modulated by means of specific O-GlcNAc transferases (OGT) as well as GlcNAcase activity that can be inhibited using the Thiamet-G (TMG) inhibitor. Mass spectrometry analysis of this modification has been complicated due to the loss of the GlcNAc group during ionization and fragmentation, but methods and technologies such as electron transfer dissociation (ETD) are opening up new avenues to study these modifications. O-GlcNAc could play an important role in many cellular processes, including metabolism, growth, morphogenesis, apoptosis, transcription, and it may play a critical role in cancer (3).
    For Research Use Only. Not For Use In Diagnostic Procedures.
    Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.
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