Abcam, ab264496, Anti-O-Linked N-Acetylglucosamine antibody [RL2] - BSA and Azide free

Size: 100µg
Mouse Monoclonal O-Linked N-Acetylglucosamine antibody. Carrier free. Suitable for WB, ICC/IF and reacts with Rat, Human samples. Cited in 1 publication.
Key facts
Host species:Mouse,
Clonality:Monoclonal,
Clone number:RL2,
Isotype:IgG1,
Light chain type:kappa,
Carrier free:Yes,
Reacts with:Rat, Human,
Applications:WB, ICC/IFSee 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.

Product details:
ab264496 is the carrier-free version of
ab2739
Want a custom formulation?
This antibody clone is manufactured by Abcam. If you require a custom buffer formulation or conjugation for your experiments, please contact orders@abcam.com
Conjugation ready
Our carrier-free antibodies are typically supplied in a PBS-only formulation, purified and free of BSA, sodium azide and glycerol. This conjugation-ready format is designed for use with fluorochromes, metal isotopes, oligonucleotides, and enzymes, which makes them ideal for antibody labelling, functional and cell-based assays, flow-based assays (e.g. mass cytometry) and Multiplex Imaging applications.
Use our
conjugation kits
for antibody conjugates that are ready-to-use in as little as 20 minutes with 1 minute hands-on-time and 100% antibody recovery: available for fluorescent dyes, HRP, biotin and gold.
Compatibility
This product is compatible with the Maxpar
Antibody Labeling Kit from Fluidigm, without the need for antibody preparation. Maxpar
is a trademark of Fluidigm Canada Inc.

Properties and Storage Information:
Form-Liquid, Purity-IgG fraction, Storage buffer-Constituents: PBS, Shipped at conditions-Blue Ice, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions-+4°C, Storage information-Do Not Freeze

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.