|Application ||WB, IHC-P, E|
|Calculated MW||49799 Da|
|Antigen Region||88-117 aa|
|Other Names||Beta-1, 3-galactosyl-O-glycosyl-glycoprotein beta-1, 6-N-acetylglucosaminyltransferase, Core 2-branching enzyme, Core2-GlcNAc-transferase, C2GNT, Core 2 GNT, GCNT1, NACGT2|
|Target/Specificity||This GCNT1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 88-117 amino acids from the Central region of human GCNT1.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||GCNT1 Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Glycosyltransferase that catalyzes the transfer of an N- acetylglucosamine moiety onto mucin-type core 1 O-glycan to form the branched mucin-type core 2 O-glycan. Mucin-type core 2 O- glycans play an important role in leukocyte extravasation as they serve as scaffolds for the display of the selectin ligand sialyl Lewis X by leukocytes.|
|Cellular Location||Golgi apparatus membrane; Single-pass type II membrane protein. Note=Also detected in the trans-Golgi network|
|Tissue Location||Highly expressed in activated T-lymphocytes and myeloid cells|
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Provided below are standard protocols that you may find useful for product applications.
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.
Bierhuizen, M.F., et al., Glycobiology 5(4):417-425 (1995).
Bierhuizen, M.F., et al., Proc. Natl. Acad. Sci. U.S.A. 89(19):9326-9330 (1992).
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