Anti-O-linked N-acetylglucosamine (O-GlcNAc) [2A8.F3] Antibody

This mouse monoclonal antibody was generated against a synthetic three-component O-linked N-acetylglucosamine (O-GlcNAc) immunogen and recognizes GluNAc pepetide/O-GlcNAc.

Highlights:

  • See full list of the O-GlcNAc Antibodies here
  • Suitable for ELISA and Western Blot applications

The study of O-GlcNAc, a ubiquitous translation and transcription regulator which is found in a wide variety of proteins, is of great relevance to multiple chronic human and veterinary diseases. These include diabetes (and its effects in the heart, kidneys and eyes), cardiovascular disease, neurodegenerative disorders involving both plaque and tangle formation, inflammatory processes, liver disease, fibrosis, metabolic disorders and cancer. There is fast growing collection of evidence that O-GlcNAcylation plays a pivotal role in epigenetics.

From the laboratories of Geert-Jan Boons, PhD, Lance Wells, PhD, and Margreet A. Wolfert, PhD University of Georgia.

Catalog Number Product Size AVAILABILITY Price Qty
EGA244
Anti-O-linked N-acetylglucosamine (O-GlcNAc) [2A8.F3] Antibody, 5mL (supernatant)
5mL (supernatant) 2-3 weeks
Price: $269.00
Specifications
Product Type: Antibody
Antigen: GlcNAc
Isotype: IgG3
Clonality: Monoclonal
Clone Name: 2A8.F3
Reactivity: GlcNAc
Immunogen: Synthetic peptide O-GlcNAc
Host: Mouse
Buffer: Cell culture supernatant
Tested Applications: ELISA, WB
Storage: -80C
Shipped: Dry Ice
Provider
From the laboratories of Geert-Jan Boons, PhD, Lance Wells, PhD, and Margreet A. Wolfert, PhD University of Georgia.
Comments

This antibody is part of a 23 Mab panel was developed specifically to study the diverse roles of O-GlcNAc and that can be employed for detection, isolation, and site localization. For details on antigen strategy, please consult: Chin Fen Teo, et al., Nat Chem Biol. 2010 May; 6(5): 338–343. doi:10.1038/nchembio.338.

See all of the O-GlcNAc Antibodies here.

References
  1. Chin Fen Teo, Sampat Ingale, Margreet A. Wolfert, Galal A. Elsayed, Laszlo G. Nöt, John C. Chatham, Lance Wells, and Geert-Jan Boons: Glycopeptide specific monoclonal antibodies suggest new roles for O-GlcNAc. Nat Chem Biol. 2010 May ; 6(5): 338–343. doi:10.1038/nchembio.338
  2. Pablo Rios, Tom S. Carter, Tiddo J. Mooibroek,* Matthew P. Crump, Micke Lisbjerg, Michael Pittelkow, Nitin T. Supekar, Geert-Jan Boons, and Anthony P. Davis: “Synthetic Receptors for the High-Affinity Recognition of O-GlcNAc Derivatives” Angew. Chem. Int. Ed. 2016, 55, 3387 –3392 http://dx.doi.org/10.1002/anie.201510611
  3. Jennifer Munkley and David J. Elliott: “Hallmarks of glycosylation in cancer”, Oncotarget, (2016)Vol. 7, No. 23, 35478-35489
  4. Peter V. Robinson, Gabriela de Almeida-Escobedo, Amber E. de Groot, Julia L. McKechnie, and Carolyn R. Bertozzi: “Live-Cell Labeling of Specific Protein Glycoforms by Proximity-Enhanced Bioorthogonal Ligation”, J. Am Chem Soc. 2015 August 26; 137(33): 10452–10455. doi:10.1021/jacs.5b04279
  5. Zhiyuan Ma and Keith Vosseller: “Cancer Metabolism and Elevated O-GlcNAc in Oncogenic Signaling”, J. Biol. Chem. VOL. 289, NO. 50, pp. 34457–34465, December 12, 2014 DOI 10.1074/jbc.R114.577718
  6. Christina M. Ferrer, Valerie L. Sodi and Mauricio J. Reginato: O-GlcNAcylation in Cancer Biology: Linking Metabolism and Signaling. J. Mol. Biol., 428(16), 3282-3294 (2016)
  7. Cheng-Xin Gong, Fei Liu, and Khalid Iqbal: O-GlcNAc cycling modulates neurodegeneration. Proc. Nat. Acad. Sci. (2012) 109(43) 17319-17320
  8. Steffi F. Baldini, Cindy Wavelet, Isabelle Hainault, Céline Guinez, Tony Lefebvre: The Nutrient-Dependent O-GlcNAc Modification Controls the Expression of Liver Fatty Acid Synthase. (2016). J. Mol. Biol., 428(16), 3295-3304
  9. Partha S. Banerjee, Olof Lagerlöf, GeraldW. Hart: Roles of O-GlcNAc in chronic diseases of aging. (2016). Molec. Aspects Med., 51, 1-15.

If you publish research with this product, please let us know so we can cite your paper.

 
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