Abcam, ab2739, Anti-O-Linked N-Acetylglucosamine antibody [RL2]

Size: 100µg
Anti-O-Linked N-Acetylglucosamine antibody [RL2] (ab2739) is a mouse monoclonal antibody detecting O-Linked N-Acetylglucosamine in Western Blot, ICC/IF . Suitable for Human, Rat . - Over 180 publications - Trusted since 2003
Key facts
Host species:Mouse,
Clonality:Monoclonal,
Clone number:RL2,
Isotype:IgG1,
Light chain type:kappa,
Carrier free:No,
Reacts with:Rat, Human,
Applications:ICC/IF, WBSee 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:
This antibody clone [RL2] is manufactured by Abcam.
If you require this antibody in a particular buffer formulation or a particular conjugate for your experiments, please contact
orders@abcam.com
or you can find further information
Product Specifications
Anti-O-Linked N-Acetylglucosamine antibody [RL2] (ab2739) is a mouse monoclonal antibody and is validated for use in ICC/IF, WB in human, rat samples.
Anti-O-Linked N-Acetylglucosamine antibody [RL2] (ab2739) specifically detects O-Linked N-Acetylglucosamine (UniProt ID: ; Molecular weight: kDa) and is sold in 100 µg selling sizes.
Quality and Validation
Abcam's high quality validation processes ensure Anti-O-Linked N-Acetylglucosamine antibody [RL2] (ab2739) has high sensitivity and specificity.
Anti-O-Linked N-Acetylglucosamine antibody [RL2] (ab2739) has been cited over 186 times in peer reviewed journals and is trusted by the scientific community.
Anti-O-Linked N-Acetylglucosamine antibody [RL2] (ab2739) has 17 independent reviews from customers.
Related Products
Conjugation-ready, carrier free format available for antibody clone RL2 -
ab288303
Antibody clone RL2 is also available pre-conjugated to a variety of labels for your convenience - Alexa Fluor® 488, Alexa Fluor® 647, HRP (
ab201993
ab201994
ab201995

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification, Storage buffer-pH: 7.4Preservative: 0.02% Sodium azideConstituents: PBS, 6.97% L-Arginine, 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.