Anti-GalNAc-T2 [UH4]

Tool Details

*FOR RESEARCH USE ONLY (for other uses, please contact the licensing team)

• Name: Anti-GalNAc-T2 [UH4]
• Alternate name: UH4, 4C4
• Research fields: Biochemistry;Cancer;Cell biology
• Tool sub type: Primary antibody
• Class: Monoclonal
• Conjugation: Unconjugated
• Strain: Balb/c
• Reactivity: Human
• Host: Mouse
• Application: ELISA ; IHC ; IF ; IP
• 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

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

Applications

• Application: ELISA ; IHC ; IF ; IP

Handling

• Format: Liquid
• Concentration: 0.9-1.1 mg/ml
• Unit size: 100 ug
• Storage buffer: PBS with 0.02% azide
• Storage conditions: -15° C to -25° C
• Shipping conditions: Shipping at 4° C

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.