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FUT8, aa32-575, Recombinant, Human (Alpha-(1,6)-fucosyltransferase, alpha1-6FucT, Fucosyltransferase 8, GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha1,6-fucosyltransferase, GDP-fucose-glycoprotein Fucosyltransferase, Glycoprotein 6-alpha-L-fucosyltransfer

Cat no: F9218-56

FUT8, aa32-575, Recombinant, Human (Alpha-(1,6)-fucosyltransferase, alpha1-6FucT, Fucosyltransferase 8, GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha1,6-fucosyltransferase, GDP-fucose-glycoprotein Fucosyltransferase, Glycoprotein 6-alpha-L-fucosyltransfer

N-glycans, O-glycans and glycolipids are frequently fucosylated at terminal sites. Therefore, fucose is often part of a sugar epitope with an important biological function. Well-known fucose-containing glycans include Lewis and ABO blood group antigens. Lewis epitopes are key elements involved in leukocyte homing and extravasation and thus are important for lymphocyte maturation and natural defense functions. Fucose-containing glycans also play critical roles in cell signaling and development (1). More than 10 fucosyltransferases have been cloned and all of them are Golgi-resident type II membrane proteins (2). FUT1 and FUT2 are a1-2 fucosyltransferases and are responsible for ABO blood-group antigen synthesis. FUT3, FUT4, FUT5, FUT6, FUT7 and FUT9 are a1-3 or a1-4 fucosyltransferases and are responsible for Lewis antigen generation (3, 4, 5). FUT8 is the only a1-6 fucosyltransferase that adds a fucose to the chitobiose core of N-glycans (6). The a1,6-fucosylation of N-glycan in human IgG1 was reported to suppress antibody-dependent cellular cytotoxicity (7, 8). Disruption of the FUT8 gene induced severe growth retardation, emphysema, and death during postnatal development in mice. The absence of a1,6-fucosylation on transforming growth facto-B1 (TGF-B1) receptors was found to be involved in the mouse phenotypes (9). The activity of this enzyme has been measured using a phosphatase-coupled assay (10).\n\nSource: \nRecombinant corresponding to aa32-575 from human FUT8, fused with 6-His tag at N-terminal, expressed in CHO cells.\n\nMolecular Weight: \n~64kD\n\nEndotoxin Level:\n(same/less than)1EU/1ug (LAL)\n\nBiological Activity:\nMeasured by its ability to hydrolyze the donor substrate GDP-fucose. The specific activity is >0.75pmoles/min/ug, as measured under the described conditions.\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Aliquots are stable for at least 6 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

F9218-56

Size

20ug

Form

Supplied as a liquid in Tris, sodium chloride.

Purity

~90% (SDS-PAGE)

References

1. Jafar-Nejad, H. et al. (2010) Glycobiology 20:931. 2. Becker, D.J. et al. (2003) Glycobiology 13:41R. 3. Blander, J. M. et al. (1999) J. Immunol. 163:3746. 4. Natsuka, S. et al. (1994) J. Biol. Chem. 269:16789. 5. Sasaki, K. et al. (1994) J. Biol. Chem. 269:14730. 6. Lee, S.H. et al. (2006) J. Biochem. 139:391. 7. Shields, R. L. et al. (2002) J. Biol. Chem. 277:26733. 8. Shinkawa, T. et al. (2003) J. Biol. Chem. 278:3466. 9. Wang, X. et al. (2005) Proc. Natl. Acad. Sci. U. S. A. 102:15791. 10. Wu, Z.L., et al. (2010) Glycobiology doi:10.1093/glycob/cwq187.

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