HPA011222
Anti-GALNT2 antibody produced in rabbit
Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution
Synonym(s):
Anti-GalNAc-T2, Anti-Polypeptide GalNAc transferase 2, Anti-Polypeptide N-acetylgalactosaminyltransferase 2, Anti-Protein-UDP acetylgalactosaminyltransferase 2, Anti-UDP- GalNAc:polypeptide N-acetylgalactosaminyltransferase 2, Anti-pp-GaNTase 2
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About This Item
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biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
product line
Prestige Antibodies® Powered by Atlas Antibodies
form
buffered aqueous glycerol solution
species reactivity
human
technique(s)
immunoblotting: 0.04-0.4 μg/mL
immunofluorescence: 0.25-2 μg/mL
immunohistochemistry: 1:50-1:200
immunogen sequence
SCKPFKWYLENVYPELRVPDHQDIAFGALQQGTNCLDTLGHFADGVVGVYECHNAGGNQEWALTKEKSVKHMDLCLTVVDRAPGSLIKLQGCRENDSRQKWEQIEGNSKLRHVGSNLCLDSRTAKSGGLSVEVCGPALSQQWKFTLNL
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... GALNT2(2590)
General description
GALNT2 (polypeptide N-acetylgalactosaminyltransferase 2) belongs to the ppGalNAc-T family, and is a type II transmembrane protein. The catalytic domain resides in the Golgi luminal region, and the R-type lectin domain lies in the C-terminal. This gene is localized to human chromosome 1q41-q42.
Immunogen
polypeptide N-acetylgalactosaminyltransferase 2
Application
Anti-GALNT2 antibody produced in rabbit, a Prestige Antibody, is developed and validated by the Human Protein Atlas (HPA) project . Each antibody is tested by immunohistochemistry against hundreds of normal and disease tissues. These images can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. The antibodies are also tested using immunofluorescence and western blotting. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit sigma.com/prestige.
Biochem/physiol Actions
GALNT2 (polypeptide N-acetylgalactosaminyltransferase 2) catalyzes the first step of O-linked glycosylation of proteins. It is responsible for the attachment of first N-acetylgalactosamine (GalNAc) monosaccharide to the protein. The expression of this gene is up-regulated in cancers, and it might be involved in tumorigenesis. It suppresses the expression of matrix metalloproteinase (MMP)-2 and transforming growth factor (TGF)-β1, and thus prevents proliferation and metastasis of gastric cancer cells. It modulates the development of placenta by regulating extravillus trophoblast (EVT) invasion. GALNT2 is also involved in insulin homeostasis by regulating the expression of ENPP1 (ectonucleotide pyrophosphatase), which is an inhibitor of insulin receptor signaling. Its expression is reduced in type 2 diabetes patients, and thus, it might play a role in hyperglycemia. It is up-regulated in oral squamous cell carcinoma (OSCC), and enhances the invasiveness of OSCC by modulating the O-glycosylation and activity of EGFR (epidermal growth factor receptor).
Features and Benefits
Prestige Antibodies® are highly characterized and extensively validated antibodies with the added benefit of all available characterization data for each target being accessible via the Human Protein Atlas portal linked just below the product name at the top of this page. The uniqueness and low cross-reactivity of the Prestige Antibodies® to other proteins are due to a thorough selection of antigen regions, affinity purification, and stringent selection. Prestige antigen controls are available for every corresponding Prestige Antibody and can be found in the linkage section.
Every Prestige Antibody is tested in the following ways:
Every Prestige Antibody is tested in the following ways:
- IHC tissue array of 44 normal human tissues and 20 of the most common cancer type tissues.
- Protein array of 364 human recombinant protein fragments.
Linkage
Corresponding Antigen APREST72034
Physical form
Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide
Legal Information
Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class
10 - Combustible liquids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Mei-Chun Lin et al.
Oral oncology, 50(5), 478-484 (2014-03-04)
Oral squamous cell carcinoma (OSCC) is one of the leading cancers worldwide. Aberrant glycosylation affects many cellular properties in cancers, including OSCC. This study aimed to explore the role of N-acetylgalactosaminyltransferase 2 (GALNT2) in OSCC. Immunohistochemistry was performed to study
Antonella Marucci et al.
PloS one, 8(7), e70159-e70159 (2013-07-31)
Impaired insulin action plays a major role in the pathogenesis of type 2 diabetes, a chronic metabolic disorder which imposes a tremendous burden to morbidity and mortality worldwide. Unraveling the molecular mechanisms underlying insulin resistance would improve setting up preventive
Wan-Ling Ho et al.
Oncotarget, 5(23), 12247-12259 (2014-11-05)
Aberrant expression of the simple mucin-type carbohydrate antigens such as Tn antigen is associated with malignant transformation and cancer progression. N-acetylgalactosaminyltransferase 2 (GALNT2), one of the enzymes that mediate the initial step of mucin-type O-glycosylation, is responsible for forming Tn
E P Bennett et al.
Glycobiology, 8(6), 547-555 (1998-06-11)
A homologous family of UDP- N -acetylgalactosamine: polypeptide N -acetylgalactosaminyltransferases (GalNAc-transferases) initiate O-glycosylation. These transferases share overall amino acid sequence similarities of approximately 45-50%, but segments with higher similarities of approximately 80% are found in the putative catalytic domain. Here
Romina B Cejas et al.
The Journal of biological chemistry, 294(9), 2997-3011 (2018-12-29)
Biological functions of nuclear proteins are regulated by post-translational modifications (PTMs) that modulate gene expression and cellular physiology. However, the role of O-linked glycosylation (O-GalNAc) as a PTM of nuclear proteins in the human cell has not been previously reported.
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