GalNAc-T3 is differentially expressed in normal tissues e.g. pancreas, kidney, reproductive and gastrointestinal tracts. GalNAc-T3 has also been implicated in spermatogenesis and carcinogenesis.
| Institute |
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| University of Copenhagen |
| SKU: | 155106 |
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| Product 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. |
| Alternate name: | UH5, 2D1 |
| Conjugation: | Unconjugated |
| Isotype: | IgG1 |
| Immunogen: | Catalytically active secreted GalNAc-T3 produced in insect cells. Recombinant protein containing aa. 52-633 (Uniprot isoform-1) |
| Immunogen Uniprot ID: | Q14435 |
| Cat. #: | 155106 |
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| Tool sub type: | Primary antibody |
| Unit size: | 100 ug |
| Research Fields: | Biochemistry; Cancer; Cell biology |
| Application: | ELISA ; IHC ; IF ; IP |
| Target: | GalNAc-T3/GALNT3 |
| Reactivity: | Human |
| Host: | Mouse |
| Class: | Monoclonal |
| 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. |
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| Format: | Liquid |
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| Concentration: | 0.9-1.1 mg/ml |
| 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. |
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