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.
The previously assigned protein identifier Q15127 has been merged into P80108. Full details can be found on the UniProt database.
Immunogen
GPLD2 (28-61) This antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide selected from the N-terminal region of human GPLD2.
Physical form
Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide.
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