05-1244 | Anti-O-GlcNAc Antibody, clone 18B10.C7(3)

100 µg  
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      Replacement Information

      Key Spec Table

      Species ReactivityKey ApplicationsHostFormatAntibody Type
      HWBMPurifiedMonoclonal Antibody
      Catalogue Number05-1244
      DescriptionAnti-O-GlcNAc Antibody, clone 18B10.C7(3)
      Alternate Names
      • O-GlcNAc transferase p110 subunit
      • O-GlcNAc transferase subunit p110
      • O-linked GlcNAc transferase
      • O-linked N-acetylglucosamine (GlcNAc) transferase (UDP-N-acetylglucosamine:polypeptide-N-acetylglucosaminyl transferase)
      • O-linked N-acetylglucosamine transferase 110 kDa subunit
      • uridinediphospho-N-acetylglucosamine:polypeptide
        beta-N-acetylglucosaminyl transferase
      Background InformationO-linked N-acetylglucosamine (O-GlcNAc), is a member of the O-GlcNAc transferase family. O-GlcNAc is a posttranslational modification characterized by the attachment of N-acetylglucosamine to specific serine/threonine hydroxyl groups. It plays an important role in nutrient sensing, gene expression, and protein degradation. O-GlcNAc is widely expressed in the pancreas and is present in smaller amounts in skeletal muscle, heart, brain and placenta.
      Product Information
      • HEK293 cell lysate
      PresentationPurified mouse monoclonal IgG1κ in buffer containing 0.1 M Tris-Glycine (pH 7.4, 150 mM NaCl) with 0.05% sodium azide.
      ApplicationAnti-O-GlcNAc Antibody, clone 18B10.C7(3) is an antibody against O-GlcNAc for use in WB.
      Key Applications
      • Western Blotting
      Biological Information
      ImmunogenSANM-conjugated linear peptide corresponding to human O-GluNAc.
      ConcentrationPlease refer to the Certificate of Analysis for the lot-specific concentration.
      SpecificityThis antibody recognizes O-GluNAc.
      Species Reactivity
      • Human
      Species Reactivity NoteProven to react with human.
      Antibody TypeMonoclonal Antibody
      Entrez Gene Number
      Entrez Gene SummaryO-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT) catalyzes the addition of a single N-acetylglucosamine in O-glycosidic linkage to serine or threonine residues. Since both phosphorylation and glycosylation compete for similar serine or threonine residues, the two processes may compete for sites, or they may alter the substrate specificity of nearby sites by steric or electrostatic effects. The protein contains nine tetratricopeptide repeats and a putative bipartite nuclear localization signal. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene. [provided by RefSeq]
      Gene Symbol
      • OGT
      • HRNT1
      • O-GLCNAC
      Purification MethodProtein G Purified
      UniProt Number
      UniProt SummaryFUNCITON: Addition of nucleotide-activated sugars directly onto the polypeptide through O-glycosidic linkage with the hydroxyl of serine or threonine. Mediates the O-glycosylation of MLL5.
      CATALYTIC ACTIVITY: UDP-N-acetyl-D-glucosamine + peptide = UDP + N-acetyl-beta-D-glucosaminyl-peptide.
      Pathway Protein modification; protein glycosylation.
      SUBUNIT STRUCTURE: Heterotrimer of two 110 kDa and one 70 kDa subunits. It is not known if the 70 kDa subunit is encoded by a separate gene or is the product of either of a proteolytic degradation or an alternative initiation of the 110 kDa subunit By similarity. Component of the MLL5-L complex, at least composed of MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with HCFC1.
      SUBCELLULAR LOCATION: Cytoplasm Potential. Nucleus Potential.
      TISSUE SPECIFICTY: Highly expressed in pancreas and to a lesser extent in skeletal muscle, heart, brain and placenta. Present in trace amounts in lung and liver.
      SEQUENCE SIMILARITIES: Belongs to the O-GlcNAc transferase family.
      Contains 13 TPR repeats.
      Molecular WeightVarious
      Physicochemical Information
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Quality AssuranceEvaluated by Western Blot in O-GlcNAc transferease transfected HEK293 cell lysate and O-GlcNAcase transfected transfected HEK293 cell lysate.

      Western Blot Analysis: 1 µg/mL of this antibody detected O-GlcNAc on 10 µg O-GlcNAc transferease transfected HEK293 cell lysate and O-GlcNAcase transfected transfected HEK293 cell lysate.
      Usage Statement
      • Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
      Storage and Shipping Information
      Storage ConditionsStable for 1 year at 2-8°C from date of receipt.
      Packaging Information
      Material Size100 µg
      Transport Information
      Supplemental Information




      Safety Data Sheet (SDS) 

      Certificates of Analysis

      TitleLot Number
      Anti-O-GlcNAc, clone 18B10.C7(3) - 2366037 2366037
      Anti-O-GlcNAc, clone 18B10.C7(3) - 2026025 2026025
      Anti-O-GlcNAc, clone 18B10.C7(3) - JBC1787357 JBC1787357
      Anti-O-GlcNAc, clone 18B10.C7(3) - NG1811494 NG1811494
      Anti-O-GlcNAc, clone 18B10.C7(3) - NG1881281 NG1881281
      Anti-O-GlcNAc, clone 18B10.C7(3) - NRG1691596 NRG1691596
      Anti-O-GlcNAc, clone 18B10.C7(3) -2709634 2709634


      Reference overviewPub Med ID
      Characterization of the specificity of O-GlcNAc reactive antibodies under conditions of starvation and stress.
      Reeves, RA; Lee, A; Henry, R; Zachara, NE
      Analytical biochemistry  457  8-18  2014

      Show Abstract
      24747005 24747005
      Antibodies that Detect O-GlcNAc on the Extracellular Domain of Cell Surface Glycoproteins.
      Tashima, Yuko and Stanley, Pamela
      J. Biol. Chem., (2014)  2014

      Show Abstract
      24573683 24573683
      Glycopeptide-specific monoclonal antibodies suggest new roles for O-GlcNAc.
      Teo, Chin Fen, et al.
      Nat. Chem. Biol., 6: 338-43 (2010)  2010

      Show Abstract
      20305658 20305658

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      Life Science Research > Antibodies and Assays > Primary Antibodies