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Anti-GalNAc-T3 [UH5] monoclonal antibody

Invented by Copenhagen Center for Glycomics, University of Copenhagen, Professor Henrik Clausen, at University of Copenhagen Copenhagen Center for Glycomics, University of Copenhagen, Associate Professor Ulla Mandel at University of Copenhagen

Info

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 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.
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

There are 8 reference entries for this reagent.

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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.


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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.


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Inventor Information

Inventors

Copenhagen Center for Glycomics, University of Copenhagen, Professor Henrik Clausen

Copenhagen Center for Glycomics, University of Copenhagen, Professor Henrik Clausen

Copenhagen Center for Glycomics, University of Copenhagen, Associate Professor Ulla Mandel

Copenhagen Center for Glycomics, University of Copenhagen, Associate Professor Ulla Mandel

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