Anti-GalNAc-T3 [UH5] monoclonal antibody
Invented by Copenhagen Center for Glycomics, University of Copenhagen, Professor Henrik Clausen , Copenhagen Center for Glycomics, University of Copenhagen, Associate Professor Ulla Mandel
Invented at University of Copenhagen
- Datasheet
- References (8)
- Inventor Info
Info
| Catalogue Number | 155106 |
| Applications | ELISA IHC IF IP |
| Antigen/Gene or Protein Targets | GalNAc-T3/GALNT3 |
| Synonyms | UH5, 2D10 |
| Reactivity | Human |
| Relevance |
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. |
| Host | Mouse |
| Immunogen | Catalytically active secreted GalNAc-T3 produced in insect cells. Recombinant protein containing aa. 52-633 (Uniprot isoform-1) |
| Immunogen UniProt ID | Q14435 |
| Subclass | IgG1 |
| Strain | Balb/c |
| Notes |
Subcellular topology of active GalNAc-T3 in cells, tissues and body fluids. UH5 2D10 tolerates fixation in ice-cold acetone and paraformaldehyde (but not methanol). UH5 2D10 does not tolerate routine FFPE methods used for histopathological archives. Incubation time is usually 2 hrs or ON. Reactivity can be easily tested by IC on air-dried, acetone fixed cells i.e. air-dry cells in PBS on multi-well slides and fix in ice-cold acetone for 8-10 min followed by drying and incubation with primary antibody. |
| Research Area | Cancer, Cell Structure and Motility, Fluorescent Cell Imaging, Structural Biology |
References: 8 entries
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.
Add a reference
References: 8 entries
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.
Add a reference
Inventor Information
Inventors
|
Copenhagen Center for Glycomics, University of Copenhagen, Professor Henrik Clausen |
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Copenhagen Center for Glycomics, University of Copenhagen, Associate Professor Ulla Mandel |
