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Contributor Information

  • Institute University of Copenhagen

Tool Details

  • Tool name: Anti-GalNAc-T2 [UH4]
  • Alternate names: UH4, 4C4
  • Tool type: Antibodies
  • Tool sub-type: Primary antibody
  • Class: Monoclonal
  • Conjugate: Unconjugated
  • Reactivity: Human
  • Host: Mouse
  • Application: ELISA ; IHC ; IF ; IP
  • Strain: Balb/c
  • Description: GalNAc-T2 is one of many polypeptide GalNAc-transferases that attach GalNAc to proteins forming the GalNAc??1-O-Ser/Thr linkage for GalNAc-type O-glycosylation. The GalNAc-transferase isoforms have considerably overlapping functions as well as unique distinct functions. GalNAc-T1 and -T2 are the main contributors to O-glycosylation of peptides in most cells and they have distinct functions as shown in murine models. GalNAc-T2 has been implicated in lipoprotein metabolism and risk of atherosclerosis as well as cancer. O-glycans are important biomarkers in cancer. The truncated O-glycans comprising Tn formed by the GalNAc transferases and T formed by further elongation by the core1 synthase (C1GalT1) are widely recognized as pancarcinoma antigens. They are masked by sialic acid or further elongation or branching in normal cells. Validation: 1. Positive reaction (IC/IF) in cells expressing GalNAc-T2 using close isoforms as negative controls e.g. GalNAc –T7/ –T10. 2. Selective IP of active GalNAc-T2 from total cell extracts. 3. Distinct perinuclear staining in cell lines (ICC/IF) and tissues (IHC, IF) suggestive of Golgi localization. 4. Loss of staining (IC/IF) following KO of GalNAc-T2
  • Immunogen: Catalytically active secreted GalNAc-T2 produced in insect cells. Recombinant protein containing aa. 52-571 (Uniprot isoform-1)
  • Immunogen UniProt ID: Q10471
  • Isotype: IgG1
  • Research area: Cancer; Cell biology; Biochemistry

  • For Research Use Only

Target Details

  • Target: GalNAc-T2/GALNT2
  • Target background: GalNAc-T2 is one of many polypeptide GalNAc-transferases that attach GalNAc to proteins forming the GalNAc1-O-Ser/Thr linkage for GalNAc-type O-glycosylation. The GalNAc-transferase isoforms have considerably overlapping functions as well as unique distinct functions. GalNAc-T1 and -T2 are the main contributors to O-glycosylation of peptides in most cells and they have distinct functions as shown in murine models. GalNAc-T2 has been implicated in lipoprotein metabolism and risk of atherosclerosis as well as cancer. O-glycans are important biomarkers in cancer. The truncated O-glycans comprising Tn formed by the GalNAc transferases and T formed by further elongation by the core1 synthase (C1GalT1) are widely recognized as pancarcinoma antigens. They are masked by sialic acid or further elongation or branching in normal cells. Validation: 1. Positive reaction (IC/IF) in cells expressing GalNAc-T2 using close isoforms as negative controls e.g. GalNAc T7/ T10. 2. Selective IP of active GalNAc-T2 from total cell extracts. 3. Distinct perinuclear staining in cell lines (ICC/IF) and tissues (IHC, IF) suggestive of Golgi localization. 4. Loss of staining (IC/IF) following KO of GalNAc-T2

Application Details

  • Application: ELISA ; IHC ; IF ; IP

Handling

  • Format: Liquid
  • Concentration: 0.9-1.1 mg/ml
  • Storage buffer: PBS with 0.02% azide
  • Storage conditions: -15°C to -25°C
  • Shipping conditions: Shipping at 4°C

Documentation

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References

  • •  A validated collection of mouse monoclonal antibodies to human glycosyltransferases functioning in mucin-type O-glycosylation.
  • •  Exploring Regulation of Protein O-Glycosylation in Isogenic Human HEK293 Cells by Differential O-Glycoproteomics.
  • •  Loss of Function of GALNT2 Lowers High-Density Lipoproteins in Humans, Nonhuman Primates, and Rodents.
  • •  Deconstruction of O-glycosylation--GalNAc-T isoforms direct distinct subsets of the O-glycoproteome.
  • •  Control of mucin-type O-glycosylation: a classification of the polypeptide GalNAc-transferase gene family.
  • •  Probing isoform-specific functions of polypeptide GalNAc-transferases using zinc finger nuclease glycoengineered SimpleCells.
  • •  Mandel et al. 1999. Glycobiology. 9(1):43-52. PMID: 9884405.
  • •  Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus.