O-GlcNAc MultiMab® Rabbit mAb mix #82332
- 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
Protocol
Specificity / Sensitivity
O-GlcNAc MultiMab® Rabbit mAb mix specifically recognizes endogenous levels of O-GlcNAc on proteins in β-O-glycosidic linkage to both serine and threonine.
Species Reactivity:
All Species Expected
The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.
Species predicted to react based on 100% sequence homology:
All Species Expected
Source / Purification
MultiMab® rabbit monoclonal mix antibodies 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
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).
Limited Uses
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