HPA011222
Anti-GALNT2 antibody produced in rabbit
Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution
Synonyme(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
Produits recommandés
Source biologique
rabbit
Conjugué
unconjugated
Forme d'anticorps
affinity isolated antibody
Type de produit anticorps
primary antibodies
Clone
polyclonal
Gamme de produits
Prestige Antibodies® Powered by Atlas Antibodies
Forme
buffered aqueous glycerol solution
Espèces réactives
human
Technique(s)
immunoblotting: 0.04-0.4 μg/mL
immunofluorescence: 0.25-2 μg/mL
immunohistochemistry: 1:50-1:200
Séquence immunogène
SCKPFKWYLENVYPELRVPDHQDIAFGALQQGTNCLDTLGHFADGVVGVYECHNAGGNQEWALTKEKSVKHMDLCLTVVDRAPGSLIKLQGCRENDSRQKWEQIEGNSKLRHVGSNLCLDSRTAKSGGLSVEVCGPALSQQWKFTLNL
Numéro d'accès UniProt
Conditions d'expédition
wet ice
Température de stockage
−20°C
Modification post-traductionnelle de la cible
unmodified
Informations sur le gène
human ... GALNT2(2590)
Description générale
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.
Immunogène
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.
Actions biochimiques/physiologiques
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).
Caractéristiques et avantages
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.
Liaison
Corresponding Antigen APREST72034
Forme physique
Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide
Informations légales
Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany
Clause de non-responsabilité
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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Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
Certificats d'analyse (COA)
Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".
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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.
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
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
Mai E Oguchi et al.
Small GTPases, 13(1), 77-83 (2021-04-17)
We have previously shown that Rab34 is an important regulator of ciliogenesis and that its unique long N-terminal region (amino acids 1-49) is essential for ciliogenesis in certain cultured mammalian cells. In the present study, we performed an in-depth deletion
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
Dong Hua et al.
International journal of molecular medicine, 30(6), 1267-1274 (2012-09-21)
Aberrant glycosylation of cell surface glycoprotein due to specific alterations of glycosyltransferase activity is usually associated with invasion and metastasis of cancer, particularly of gastric carcinomas. Polypeptide N-acetylgalactosaminyltransferase 2 (ppGalNAc-T2), which catalyzes initiation of mucin-type O-glycosylation, is also involved in
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