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Hamster FUT8 Protein (aa 68-575, His Tag)

FUT8

Catalog Number P51166-M08B
Organism Species Hamster
Host Baculovirus-Insect Cells
Synonyms FUT8
Molecular Weight The recombinant hamster FUT8 consists of 518 amino acids and has a calculated molecular mass of 60.1 kDa. The recombinant protein migrates as an approximately 55 kDa band in SDS-PAGE under reducing conditions.
predicted N Arg 575
SDS-PAGE
Purity > 95 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the hamster FUT8 (G3HCE4) (Arg68-Lys575) was fused with a polyhistidine tag at the C-terminus.
Bio-activity
Research Area Signaling |Signal Transduction |Metabolism |Types of disease |Metabolism in Cancer
Formulation Lyophilized from sterile 20mM Tris, 500mM NaCl, 3mM DTT, 10% glycerol, pH 7.0.
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background Human alpha (1,6) fucosyltransferase 8, also known as FUT8, is a member of the glycosyltransferase family. Fucosyltransferases are the enzymes transferring fucose from GDP-Fuc to Gal in an alpha1,2-linkage and to GlcNAc in alpha1,3-linkage, alpha1,4-linkage, or alpha1,6-linkage. All fucosyltransferases utilize the same nucleotide sugar, their specificity reside in the recognition of the acceptor and in the type of linkage formed. Fucosyltransferases share some common structural and catalytic features. On the basis of protein sequence similarities, these enzymes can be classified into four distinct families: (1) the alpha-2-fucosyltransferases, (2) the alpha-3-fucosyltransferases, (3) the mammalian alpha-6-fucosyltransferases, and (4) the bacterial alpha-6-fucosyltransferases. The alpha-3-fucosyltransferases constitute a distinct family as they lack the consensus peptide, but some regions display similarities with the alpha-2 and alpha-6-fucosyltranferases.
Reference
  • Breton C, et al. (1998) Conserved structural features in eukaryotic and prokaryotic fucosyltransferases. Glycobiology. 8(1): 87-94.
  • Oriol R, et al. (1999) Divergent evolution of fucosyltransferase genes from vertebrates, invertebrates, and bacteria. Glycobiology. 9(4): 323-34.
  • de Vries T, et al. (2001) Fucosyltransferases: structure / function studies. Glycobiology. 11(10): 119-128.
  • Baboval T, et al. (2002) Comparison of human and mouse Fuc-TX and Fuc-TXI genes, and expression studies in the mouse. Mamm Genome. 13(9): 538-41.