Glyko® α(1-2,3,4,6) Fucosidase [GKX-5006]

$ 400.00


Broad specificity; releases non-reducing terminal α(1-2,3,4,6)-linked fucose from N- and O-glycans. Cleaves α(1-6) core fucose (linked to the innermost GlcNAc of N-glycans) more efficiently than other α-fucose linkages.

Bovine kidney.

The enzyme has broad substrate specificity, cleaving α(1-2,3,4,6)-linked fucose from N- and O-glycans. It cleaves α(1-6) linked fucose on the trimannosyl core of N-linked oligosaccharides more efficiently than other α-fucose linkages. The fine specificity of the enzyme is complicated since the aglycon portion of the substrate significantly influences the substrate kinetics. The rate of cleavage is lower with increasing oligosaccharide size and complexity.


Figure 1: Cleavage specificity for GKX-5006 α(1-2,3,4,6) Fucosidase.

Bovine derived α-fucosidase has been extensively used in the sequence analysis of N-glycans. It has also been used for analysis and modification of glycoconjugates including blood group oligosaccharides and glycolipids.

Ships with: 
WS0122 Buffer [500 mM sodium citrate/phosphate pH 6.0, 250 ug/ml BSA]

Reaction Buffer:
5X concentrated buffer which when diluted gives 100 mM sodium citrate phosphate pH 6.0.

Lyophilized from 20 mM sodium citrate phosphate, 0.25 mg/ml BSA (pH 6.0)

MW: 210-220 kD 

pH optimum/range:

Unit Definition:
One unit is defined as the amount of enzyme required to hydrolyze 1 μmole of pNP-α-fucopyranoside per minute at pH 6.0 and 37°C.

Size: 500 mU lyophilized

Product Code: GKX-5006


Q. Can I use this enzyme to remove core (α-1,6 linked) fucose from the N-glycans of intact glycoproteins such as IgG?

A. Using bovine kidney fucosidase (GKX-5006) to remove core fucose from an N-glycan while the glycan is still attached to an intact IgG is likely to be difficult, due to steric hindrance. For example, bovine kidney fucosidase has been shown to be ineffective at removing core fucose from the N-glycans of intact rituximab [1]. 

Absence of core fucose on the N-glycans of therapeutic antibodies enhances antibody-dependent cellular toxicity (ADCC) [2], and this has spurred interest in other approaches to controlling antibody fucosylation [3], including the use of cell lines with altered fucosylation pathways.

  1. Huang W, Giddens J, Fan SQ, Toonstra C, Wang LX. Chemoenzymatic glycoengineering of intact IgG antibodies for gain of functions.  2012 Jul 25;134(29):12308-18.
  2. Shields RL, Lai J, Keck R, O’Connell LY, Hong K, Meng YG, Weikert SH, Presta LG. Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity.  2002 Jul 26;277(30):26733-40.
  3. Yamane-Ohnuki N, Satoh M. Production of therapeutic antibodies with controlled fucosylation.  2009 May-Jun;1(3):230-6.
Product Citations
  1. Hasehira K, Tateno H, Onuma Y, Ito Y, Asashima M, Hirabayashi J.  Structural and quantitative evidence for dynamic glycome shift on production of induced pluripotent stem cells.   2012 Dec;11(12):1913-23.
  2. Huang W, Giddens J, Fan SQ, Toonstra C, Wang LX.  Chemoenzymatic glycoengineering of intact IgG antibodies for gain of functions.   2012 Jul 25;134(29):12308-18.
  3. Storr SJ, Royle L, Chapman CJ, Hamid UM, Robertson JF, Murray A, Dwek RA, Rudd PM.  The O-linked glycosylation of secretory/shed MUC1 from an advanced breast cancer patient's serum.   2008 Jun;18(6):456-62.
  4. Hershkovitz O, Jarahian M, Zilka A, Bar-Ilan A, Landau G, Jivov S, Tekoah Y, Glicklis R, Gallagher JT, Hoffmann SC, Zer H, Mandelboim O, Watzl C, Momburg F, Porgador A.  Altered glycosylation of recombinant NKp30 hampers binging to heparan sulfate: a lesson for the use of recombinant immunoreceptors as an immunological tool.   2008 Jan;18(1):28-41.
  5. Shaaltiel Y, Bartfield D, Hashmueli S, Baum G, Brill-Almon E, Galili G, Dym O, Boldin-Adamsky SA, Silman I, Sussman JL, Futerman AH, Aviezer D.  Production of glucocerebrosidase with terminal mannose glycans for enzyme replacement therapy of Gaucher's disease using a plant cell system.   2007 Sep;5(5):579-90.
  6. Sandra K, Dolashka-Angelova P, Devreese B, Van Beeumen J.  New insights in Rapana venosa hemocyanin N-glycosylation resulting from on-line mass spectrometric analyses.   2007 Feb;17(2):141-56.
  7. Jayachandran R, Radcliffe CM, Royle L, Harvey DJ, Dwek RA, Rudd PM, Karande AA.  Oligosaccarides modulate the apoptotic activity of glycodelin.   2006 Nov;16(11):1052-63.

Product Safety Documentation for GKX-5006:

Product/Part No. Description
GKX-5006 Glyko® α(1-2,3,4,6) Fucosidase (bovine kidney) 

US-5x Reaction Buffer

GB-5x Reaction Buffer

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