O-linked N-acetylglucosamine (O-GlcNAc) Monoclonal Antibody (HGAC85)

This webpage contains legacy information. The product is either no longer available from the supplier or has been delisted at Labome.

product summary

company name :

Invitrogen

other brands :

NeoMarkers, Lab Vision, Endogen, Pierce, BioSource International, Zymed Laboratories, Caltag, Molecular Probes, Research Genetics, Life Technologies, Applied Biosystems, GIBCO BRL, ABgene, Dynal, Affinity BioReagents, Nunc, Invitrogen, NatuTec, Oxoid, Richard-Allan Scientific, Arcturus, Perseptive Biosystems, Proxeon, eBioscience

product type :

antibody

product name :

O-linked N-acetylglucosamine (O-GlcNAc) Monoclonal Antibody (HGAC85)

catalog :

MA1-076

quantity :

100 uL

price :

US 471.00

clonality :

monoclonal

host :

mouse

conjugate :

nonconjugated

clone name :

HGAC85

reactivity :

human, mouse, rat

application :

western blot, ELISA, immunohistochemistry, immunocytochemistry, immunoprecipitation, chromatin immunoprecipitation

citations: 21

Reference
Na H, Abramowitz L, Hanover J. Cytosolic O-GlcNAcylation and PNG1 maintain Drosophila gut homeostasis by regulating proliferation and apoptosis. PLoS Genet. 2022;18:e1010128 pubmed publisher
Akan I, Halim A, Vakhrushev S, Clausen H, Hanover J. Drosophila O-GlcNAcase Mutants Reveal an Expanded Glycoproteome and Novel Growth and Longevity Phenotypes. Cells. 2021;10: pubmed publisher
Boulard M, Rucli S, Edwards J, Bestor T. Methylation-directed glycosylation of chromatin factors represses retrotransposon promoters. Proc Natl Acad Sci U S A. 2020;117:14292-14298 pubmed publisher
Na H, Akan I, Abramowitz L, Hanover J. Nutrient-Driven O-GlcNAcylation Controls DNA Damage Repair Signaling and Stem/Progenitor Cell Homeostasis. Cell Rep. 2020;31:107632 pubmed publisher
Shiou Y, Lin H, Ke L, Wu B, Shin S, Chen C, et al. Very Low-Density Lipoproteins of Metabolic Syndrome Modulates STIM1, Suppresses Store-Operated Calcium Entry, and Deranges Myofilament Proteins in Atrial Myocytes. J Clin Med. 2019;8: pubmed publisher
Krause M, Love D, Ghosh S, Wang P, Yun S, Fukushige T, et al. Nutrient-Driven O-GlcNAcylation at Promoters Impacts Genome-Wide RNA Pol II Distribution. Front Endocrinol (Lausanne). 2018;9:521 pubmed publisher
Lee H, Chen C, Tsai W, Lin H, Shiao Y, Sheu S, et al. Very-Low-Density Lipoprotein of Metabolic Syndrome Modulates Gap Junctions and Slows Cardiac Conduction. Sci Rep. 2017;7:12050 pubmed publisher
Akan I, Love D, Harwood K, Bond M, Hanover J. Drosophila O-GlcNAcase Deletion Globally Perturbs Chromatin O-GlcNAcylation. J Biol Chem. 2016;291:9906-19 pubmed publisher
Tashima Y, Stanley P. Antibodies that detect O-linked ?-D-N-acetylglucosamine on the extracellular domain of cell surface glycoproteins. J Biol Chem. 2014;289:11132-42 pubmed publisher
Miura Y, Sakurai Y, Endo T. O-GlcNAc modification affects the ATM-mediated DNA damage response. Biochim Biophys Acta. 2012;1820:1678-85 pubmed publisher
Love D, Ghosh S, Mondoux M, Fukushige T, Wang P, Wilson M, et al. Dynamic O-GlcNAc cycling at promoters of Caenorhabditis elegans genes regulating longevity, stress, and immunity. Proc Natl Acad Sci U S A. 2010;107:7413-8 pubmed publisher
Hamiel C, Pinto S, Hau A, Wischmeyer P. Glutamine enhances heat shock protein 70 expression via increased hexosamine biosynthetic pathway activity. Am J Physiol Cell Physiol. 2009;297:C1509-19 pubmed publisher
Paton L, Gerrard J, Bryson W. Investigations into charge heterogeneity of wool intermediate filament proteins. J Proteomics. 2008;71:513-29 pubmed publisher
Robles Flores M, Meléndez L, Garcia W, Mendoza Hernandez G, Lam T, Castañeda Patlán C, et al. Posttranslational modifications on protein kinase c isozymes. Effects of epinephrine and phorbol esters. Biochim Biophys Acta. 2008;1783:695-712 pubmed publisher
Andrali S, Qian Q, Ozcan S. Glucose mediates the translocation of NeuroD1 by O-linked glycosylation. J Biol Chem. 2007;282:15589-96 pubmed
Cameron R, Liu C, Mixon A, Pihkala J, Rahn R, Cameron P. Myosin16b: The COOH-tail region directs localization to the nucleus and overexpression delays S-phase progression. Cell Motil Cytoskeleton. 2007;64:19-48 pubmed
Sima A, Zhang W, Li Z, Murakawa Y, Pierson C. Molecular alterations underlie nodal and paranodal degeneration in type 1 diabetic neuropathy and are prevented by C-peptide. Diabetes. 2004;53:1556-63 pubmed
Zhu W, Leber B, Andrews D. Cytoplasmic O-glycosylation prevents cell surface transport of E-cadherin during apoptosis. EMBO J. 2001;20:5999-6007 pubmed
Zhang X, Bennett V. Identification of O-linked N-acetylglucosamine modification of ankyrinG isoforms targeted to nodes of Ranvier. J Biol Chem. 1996;271:31391-8 pubmed
Nahm M, Clevinger B, Davie J. Monoclonal antibodies to streptococcal group A carbohydrate. I. A dominant idiotypic determinant is located on Vk. J Immunol. 1982;129:1513-8 pubmed
Holt G, Snow C, Senior A, Haltiwanger R, Gerace L, Hart G. Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine. J Cell Biol. 1987;104:1157-64 pubmed

product information

Product Type :

Antibody

Product Name :

O-linked N-acetylglucosamine (O-GlcNAc) Monoclonal Antibody (HGAC85)

Catalog # :

MA1-076

Quantity :

100 uL

Price :

US 471.00

Clonality :

Monoclonal

Host :

Mouse

Reactivity :

Chemical

Applications :

ELISA: Assay-dependent, Immunocytochemistry: 1:250, Immunoprecipitation: Assay-dependent, Western Blot: 1:250-1:1,000

Species :

Chemical

Clone :

HGAC85

Isotype :

IgG3

Storage :

-20 C, Avoid Freeze/Thaw Cycles

Description :

O-linked N-acetylglucosamine (O-GlcNAc) is a posttranslational modification characterized by the attachment of N-acetylglucosamine to specific serine or threonine residues. Unlike other protein glycosylations, O-GlcNAc modifications occur within the nucleus and cytoplasm. They are found on many cellular proteins, including nuclear pore, oncogene, cytoskeletal, heat shock, viral and transcription regulatory proteins. O-GlcNAc glycosylations are thought to obscure phosphorylation sites, counteracting phosphorylation-dependent signaling pathways and protein interactions.

Immunogen :

Heat killed, pepsin treated group A streptococci.

Format :

Liquid

Applications w/Dilutions :

ELISA: Assay-dependent, Immunocytochemistry: 1:250, Immunoprecipitation: Assay-dependent, Western Blot: 1:250-1:1,000

Aliases :

GlcNAc; HINCUT-1; HRNT1; O-GLCNAC; O-GlcNAc transferase p110 subunit; O-GlcNAc transferase subunit p110; OGT; O-linked N-acetylglucosamine (GlcNAc) transferase; O-linked N-acetylglucosamine (GlcNAc) transferase (UDP-N-acetylglucosamine:polypeptide-N-acetylglucosaminyl transferase); O-linked N-acetylglucosamine transferase 110 kDa subunit; UDP-N-acetylglucosamine:polypeptide-N-acetylglucosaminyl transferase; UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit; uridinediphospho-N-acetylglucosamine:polypeptide beta-N-acetylglucosaminyl transferase