Anti-GalNAc-T3 [UH5]

Tool Details

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

• Name: Anti-GalNAc-T3 [UH5]
• Alternate name: UH5, 2D1
• 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-T3 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-T3 is differentially expressed in normal tissues e.g. pancreas, kidney, reproductive and gastrointestinal tracts. Genetic deficiency in GalNAc-T3 results in familial tumoral calcinosis and hyperostosis hyperphosphatemia syndrome due to lack of O-glycosylation of FGF23, which is a key regulator of serum phosphate homeostasis. GalNAc-T3 has also been implicated in spermatogenesis and carcinogenesis. 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-T3 using close isoforms as negative controls e.g. GalNAc-T6. 2. Selective IP of active GalNAc-T3 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-T3.
• Immunogen: Catalytically active secreted GalNAc-T3 produced in insect cells. Recombinant protein containing aa. 52-633 (Uniprot isoform-1)
• Immunogen uniprot id: Q14435
• Isotype: IgG1

Target Details

• Target: GalNAc-T3/GALNT3
• Target background: GalNAc-T3 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-T3 is differentially expressed in normal tissues e.g. pancreas, kidney, reproductive and gastrointestinal tracts. Genetic deficiency in GalNAc-T3 results in familial tumoral calcinosis and hyperostosis hyperphosphatemia syndrome due to lack of O-glycosylation of FGF23, which is a key regulator of serum phosphate homeostasis. GalNAc-T3 has also been implicated in spermatogenesis and carcinogenesis. 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-T3 using close isoforms as negative controls e.g. GalNAc-T6. 2. Selective IP of active GalNAc-T3 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-T3.

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: Dry ice

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.
• Expression of the O-Glycosylation Enzyme GalNAc-T3 in the Equatorial Segment Correlates with the Quality of Spermatozoa.
• 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.
• Polypeptide GalNAc-transferase T3 and familial tumoral calcinosis. Secretion of fibroblast growth factor 23 requires O-glycosylation.
• Mandel et al. 1999. Glycobiology. 9(1):43-52. PMID: 9884405.
• cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D-galactosamine. Polypeptide N-acetylgalactosaminyltransferase, GalNAc-t3.