Abcam, ab201994, Alexa Fluor® 647 Anti-O-Linked N-Acetylglucosamine antibody [RL2]

Size: 100µL
Mouse Monoclonal O-Linked N-Acetylglucosamine antibody - conjugated to Alexa Fluor® 647. Suitable for ICC/IF and reacts with Human samples. Cited in 1 publication.
Key facts
Host species:Mouse,
Clonality:Monoclonal,
Clone number:RL2,
Isotype:IgG1,
Conjugation:Alexa Fluor® 647,
Excitation/Emission:Ex: 650nm, Em: 665nm,
Carrier free:No,
Reacts with:Human,
Applications:ICC/IFSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.

Product details:
Alexa Fluor® is a registered trademark of Molecular Probes, Inc, a Thermo Fisher Scientific Company. The Alexa Fluor® dye included in this product is provided under an intellectual property license from Life Technologies Corporation. As this product contains the Alexa Fluor® dye, the purchase of this product conveys to the buyer the non-transferable right to use the purchased product and components of the product only in research conducted by the buyer (whether the buyer is an academic or for-profit entity). As this product contains the Alexa Fluor® dye the sale of this product is expressly conditioned on the buyer not using the product or its components, or any materials made using the product or its components, in any activity to generate revenue, which may include, but is not limited to use of the product or its components: in manufacturing; (ii) to provide a service, information, or data in return for payment (iii) for therapeutic, diagnostic or prophylactic purposes; or (iv) for resale, regardless of whether they are sold for use in research. For information on purchasing a license to this product for purposes other than research, contact Life Technologies Corporation, 5781 Van Allen Way, Carlsbad, CA 92008 USA or outlicensing@thermofisher.com.

Properties and Storage Information:
Form-Liquid, Purity-IgG fraction, Storage buffer-pH: 7.4Preservative: 0.02% Sodium azideConstituents: PBS, 30% Glycerol (glycerin, glycerine), 1% 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, Store in the dark

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.