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PNGase F

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Recombinant Proteins

Cat. No. Product Name Target Research Areas Chemical Structure
  • HY-P2929
    PNGase F
    1 Publications Verification

    		 Biochemical Assay Reagents Glycosidase Cancer
    PNGase F, a glycosidase, catalyzes the cleavage of an internal glycoside bond in an oligosaccharide. PNGase F removes nearly all N-linked oligosaccharides from glycoproteins. PNGase F can release N-glycans from glycoproteins in glycoanalytical workflows .
    PNGase F
  • HY-P2929A
    PNGase F-Fast
    1 Publications Verification

    		 Glycosidase Cancer
    PNGase F-Fast is a glycosidase that catalyzes the cleavage of internal glycosidic bonds in oligosaccharides. PNGase F-Fast removes almost all N-linked oligosaccharides from glycoproteins. PNGase F-Fast can release N-glycans from glycoproteins in the sugar analysis workflow. The cleavage site is: the glycosidic bond between the innermost N-acetylglucosamine and asparagine. PNGase F-Fast is an improved reagent that allows for rapid deglycosylation of antibodies and antibody fusions within minutes .
    PNGase F-Fast
  • HY-P2929B
    PNGase F (Immobilized, Microspin)

    		Glycosidase Cancer
    PNGase F (Immobilized, Microspin) is a resin in which the PNGase F (peptide N-glycosidase F) enzyme is covalently coupled to agarose beads for the removal of N-glycans from antibodies, fusion proteins, and other N-glycosylated proteins. The enzyme is recombinantly expressed in E.coli and the sequence is derived from Flavobacterium meningsepticum .
    PNGase F (Immobilized, Microspin)

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