ANTIBODIES

Contributor Information
- Institute University of Copenhagen
Tool Details
- Tool name: Anti-GalNAc-T3 [UH5]
- Alternate names: UH5, 2D1
- 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-T3 is one of many polypeptide GalNAc-transferases that attach GalNAc to proteins forming the GalNAc?ĂÂ?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
- Research area: Cancer; Cell biology; Biochemistry
- For Research Use Only
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.
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: -15ðC to -25ðC
- Shipping conditions: Shipping at 4ðC
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.