Anti-GalNAc-T2 [UH4] 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 | 155105 |
| Applications | ELISA IHC IF IP |
| Antigen/Gene or Protein Targets | GalNAc-T2/GALNT2 |
| Synonyms | UH4, 4C4 |
| Reactivity | Human |
| Relevance |
GalNAc-T2 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-T1 and -T2 are the main contributors to O-glycosylation of peptides in most cells and they have distinct functions as shown in murine models. GalNAc-T2 has been implicated in lipoprotein metabolism and risk of atherosclerosis as well as cancer. 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-T2 using close isoforms as negative controls e.g. GalNAc –T7/ –T10. 2. Selective IP of active GalNAc-T2 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-T2 |
| Host | Mouse |
| Immunogen | Catalytically active secreted GalNAc-T2 produced in insect cells. Recombinant protein containing aa. 52-571 (Uniprot isoform-1) |
| Immunogen UniProt ID | Q10471 |
| Subclass | IgG1 |
| Strain | Balb/c |
| Notes |
UH4 4C4 can be used to probe subcellular topology of active GalNAc-T2 in cells and tissues as well as its presence in body fluids. UH4 4C4 tolerates fixation in ice-cold acetone and paraformaldehyde (but not methanol). UH4 4C4 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.
Loss of Function of GALNT2 Lowers High-Density Lipoproteins in Humans, Nonhuman Primates, and Rodents.
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.
Probing isoform-specific functions of polypeptide GalNAc-transferases using zinc finger nuclease glycoengineered SimpleCells.
Mandel et al. 1999. Glycobiology. 9(1):43-52. PMID: 9884405.
Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus.
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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.
Loss of Function of GALNT2 Lowers High-Density Lipoproteins in Humans, Nonhuman Primates, and Rodents.
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.
Probing isoform-specific functions of polypeptide GalNAc-transferases using zinc finger nuclease glycoengineered SimpleCells.
Mandel et al. 1999. Glycobiology. 9(1):43-52. PMID: 9884405.
Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus.
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 |
