Beta-1,3-Galactosyl-O-Glycosyl-Glycoprotein Beta-1,6-N-Acetylglucosaminyltransferase (GCNT1) Antibody

Product specifications

Primary Antibodies

Beta-1,3-Galactosyl-O-Glycosyl-Glycoprotein Beta-1,6-N-Acetylglucosaminyltransferase (GCNT1)

Rabbit

Human

WB: 1/500 - 1/2000. Optimal dilutions/concentrations should be determined by the end user.

Polyclonal

Unconjugated

IgG

Purified by affinity chromatography.

60 µl

120 µl

200 µl

Liquid

WB

PBS, pH 7.3, containing 0.01% thiomersal, 50% glycerol.

Shipped within 5-10 working days.

Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles.

No

Q02742

2650

NP_001091103.1

G6NT,C2GNT,C2GNT1,NACGT2,NAGCT2,C2GNT-L,C2GlcNAcT

Antibody anti-GCNT1

RUO

Concentration: 1 mg/ml -

Descripción

Glucosaminyl (N-acetyl) transferase 1 (GCNT1) is a glycosyltransferase that catalyzes the addition of N-acetylglucosamine to mucin-type O-glycans, forming core 2 and core 4 branched structures critical for glycoprotein biosynthesis GCNT1 plays a key role in the synthesis of mucins, which protect epithelial barriers in the gastrointestinal and respiratory tracts by regulating mucus production and cell adhesion It is expressed in various tissues, particularly those with high mucus turnover, and is vital for immune responses and cellular signaling Dysregulation of GCNT1 has been associated with cancer progression, especially in breast and gastrointestinal cancers, where aberrant glycosylation promotes tumor invasion and metastasis Additionally, GCNT1 contributes to inflammatory diseases, impacting immune cell trafficking and epithelial defense pathways Studies highlight its involvement in maintaining epithelial integrity and its therapeutic potential as a target for diseases characterized by disrupted glycosylation patterns

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Beta-1,3-Galactosyl-O-Glycosyl-Glycoprotein Beta-1,6-N-Acetylglucosaminyltransferase (GCNT1) Antibody

This gene is a member of the beta-1, 6-N-acetylglucosaminyltransferase gene family. It is essential to the formation of Gal beta 1-3 (GlcNAc beta 1-6) GalNAc structures and the core 2 O-glycan branch. The gene coding this enzyme was originally mapped to 9q21, but was later localized to 9q13. Multiple alternatively spliced variants, encoding the same protein, have been identified.

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Beta-1,3-Galactosyl-O-Glycosyl-Glycoprotein Beta-1,6-N-Acetylglucosaminyltransferase (GCNT1) Antibody

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Glycosylation is one of the most universal but at the same time complex protein modifications. Modification with sugar moeties can be both co translational and post translational, occurring in the endoplasmatic reticulum and golgi. Three different forms of glycosylation can be distinguished: N-linked oligosaccharides, O-linked oligosaccharides and glycosyl phosphatidylinositol (GPI-) anchors. Glycosylation results in thousands of distinct, bioactive glycoproteins resident throughout the cell that strongly determine protein-protein, carbohydrate-protein, membrane, and adhesion properties. Diseases associated with glycosylation defects include Congenital disorders of glycosylation, (CDG), also known as carbohydrate deficient glycoprotein syndromes, and diseases associated with advanced aging.

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