Abcam, ab202665, Anti-O-Linked N-Acetylglucosamine antibody [EPR19847]

Size: 100µL / 1mL
Rabbit Recombinant Monoclonal O-Linked N-Acetylglucosamine antibody. Suitable for IP, Dot, WB and reacts with Human, Rat, Synthetic peptide samples. Cited in 1 publication.
Key facts
Host species:Rabbit,
Clonality:Monoclonal,
Clone number:EPR19847,
Isotype:IgG,
Carrier free:No,
Reacts with:Rat, Human,
Applications:IP, WB, DotSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:The exact immunogen used to generate this antibody is proprietary information.,
Specificity:This product is recommended in human and rat and is not suitable for mouse. Cross-reactivity with other species has not been confirmed experimentally.

Product details:
Patented technology
Our RabMAb
technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to
RabMAb® patents
What are the advantages of a recombinant monoclonal antibody?
This product is a recombinant monoclonal antibody, which offers several advantages including:
- High batch-to-batch consistency and reproducibility
- Improved sensitivity and specificity
- Long-term security of supply
- Animal-free batch production
For more information, read more on
recombinant antibodies

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Protein A, Storage buffer-pH: 7.2 - 7.4Preservative: 0.01% Sodium azideConstituents: PBS, 40% Glycerol (glycerin, glycerine), 0.05% BSA, Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
O-Linked N-Acetylglucosamine (O-GlcNAc) is a post-translational modification involving the addition of a single N-acetylglucosamine moiety to the serine or threonine residues of nuclear and cytoplasmic proteins. This dynamic modification is sometimes referred to as O-GlcNAcylation. The molecular mass of the O-GlcNAc group itself is approximately 203 Da. This modification is expressed widely across various tissues notably in the brain and pancreas. O-GlcNAc plays a critical role in regulating protein function stability and interaction.
Biological function summary
O-GlcNAc modifies proteins influencing cellular processes such as transcription signal transduction and stress response. It is involved in the regulation of transcription factors like Sp1 and NF-kB and is associated with the O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) enzymes which respectively add and remove the GlcNAc group. O-GlcNAc functions in a manner similar to phosphorylation often competing with it on the same or adjacent serine/threonine sites. This modification is not part of a permanent protein complex but dynamically modulates protein interactions and activity.
Pathways
This modification plays a fundamental role in pathways related to nutrient sensing and insulin signaling. It modulates proteins such as insulin receptor substrate 1 (IRS1) and Akt to link nutrient status to cellular responses. The hexosamine biosynthetic pathway (HBP) is an important pathway in which O-GlcNAc is synthesized. Through these pathways it impacts cellular signaling and metabolism influencing processes like cellular growth and apoptosis.
O-GlcNAc modification connects to conditions like diabetes and Alzheimer's disease. Elevated O-GlcNAc levels contribute to insulin resistance a hallmark of type 2 diabetes through interaction with proteins such as IRS1 and Akt. In Alzheimer's O-GlcNAc modifies tau protein reducing its phosphorylation and aggregation therefore potentially affecting neurofibrillary tangle formation. These connections underline the importance of O-GlcNAc in the pathophysiology of these diseases and highlight its potential as a therapeutic target.