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Since the phenotype of the Nias patients differs from the Larsen-like syndrome described for patients with mutation p.(Arg277Gln), we suggest mutation B3GAT3:p.(Pro140Leu) to cause a different type of GAG linkeropathy showing no involvement of the heart.
Reduced GlcAT-I activity impairs skeletal as well as heart development and results in variable combinations of heart malformations.
functional glycosyltransferase signature sequence of the human beta 1,3-glucuronosyltransferase is a XDD motif
we evaluated the consequences of C-4/C-6 sulfation of Galbeta1-3Gal (Gal2 (show GAL2 ELISA Kits)-Gal1 (show LGALS1 ELISA Kits)) on the activity and specificity of beta1,3-glucuronosyltransferase I
GlcAT-I has a role in controlling and reversing articular cartilage defects
A comparison of substrate specificity of beta1,3-glucuronosyltransferases revealed that GlcAT-I was selective toward Galbeta1,3Gal, whereas GlcAT-P (show B3GAT1 ELISA Kits) presented a broader profile.
2-o-phosphorylation of xylose and 6-o-sulfation of galactose in the protein linkage region of glycosaminoglycans influence the glucuronyltransferase-I activity involved in the linkage region synthesis
mice with a deletion of GlcAT-I showed remarkable reduction of the synthesis of chondroitin sulfate and heparan sulfate and embryonic lethality before the 8-cell stage because of failed cytokinesis
The protein encoded by this gene is a member of the glucuronyltransferase gene family, enzymes that exhibit strict acceptor specificity, recognizing nonreducing terminal sugars and their anomeric linkages. This gene product catalyzes the formation of the glycosaminoglycan-protein linkage by way of a glucuronyl transfer reaction in the final step of the biosynthesis of the linkage region of proteoglycans.
, UDP-GlcUA:Gal beta-1,3-Gal-R glucuronyltransferase
, galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3
, glucuronosyltransferase I
, glucuronyltransferase I