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HPA011222

Sigma-Aldrich

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

UNSPSC Code:
12352203
Human Protein Atlas Number:
NACRES:
NA.41

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:
  • 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 Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

HPA011222-100UL:
HPA011222-25UL:


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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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
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
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
Laura Hobohm et al.
Cellular and molecular life sciences : CMLS, 79(3), 185-185 (2022-03-14)
Golgi membrane proteins such as glycosyltransferases and other glycan-modifying enzymes are key to glycosylation of proteins and lipids. Secretion of soluble Golgi enzymes that are released from their membrane anchor by endoprotease activity is a wide-spread yet largely unexplored phenomenon.

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