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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning and expression of human membrane beta1,4-GalT7 in HeLa cells, expression of soluble form as a fusion protein with maltose-binding protein in Escherichia coli
expression of a hybrid enzyme (called xylGalT), consisting of the N-terminal domain of Arabidopsis thaliana xylosyltransferase and the catalytic domain of human beta-1,4-galactosyltransferase I (GalT) in tobacco causes a sharp reduction of N-glycans with potentially immunogenic corebound xylose (Xyl) and fucose (Fuc) residues
gene B4GALT7, recombinant expression of GST-tagged wild-type and mutant enzymes in CHOpgsB-618 cells, recombinant expression of the soluble GST-tagged mutant enzyme in Escherichia coli strain BL21(DE3)
gene CGI_10013446, transcriptome screening and DNA and amino acid sequence determination and analysis, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
mutated beta1,4-GalT7s are expressed as soluble maltose-binding protein fusions in which the N-terminal cytoplasmic domain, the transmembrane segment and the stem region, which precede the catalytic domain and correspond to amino acids 1-81, are deleted