B3GAT3 Human

B3GAT3 is a type II transmembrane protein that comprises 335 amino acids and includes one N-glycan . The enzyme has a molecular mass of approximately 37 kDa, which increases to around 47 kDa upon glycosylation . The structure of B3GAT3 includes a proline-rich domain near the transmembrane region, which is a characteristic feature shared with other glycosyltransferases .

The enzyme’s primary function is to catalyze the formation of the glycosaminoglycan-protein linkage region. This involves transferring a glucuronic acid (GlcA) from UDP-GlcA to the trisaccharide-serine sequence, Galβ1-3Galβ1-4Xylβ1-O-Ser . This linkage region is common to various proteoglycans, including heparan sulfate and chondroitin sulfate proteoglycans .

B3GAT3 is essential for the proper synthesis of heparan sulfate and chondroitin sulfate, which are critical for various biological processes, including cell division, cell signaling, and the maintenance of tissue structure . Knockout studies in mice have shown that the absence of B3GAT3 leads to embryonic lethality before the 8-cell stage due to failed cytokinesis, highlighting the enzyme’s critical role in embryonic development .

Recombinant human B3GAT3 is produced using advanced biotechnological methods to ensure high purity and activity. It is typically supplied as a carrier-free, 0.2 μm filtered solution in Tris and NaCl . The recombinant form is used in various research applications, including enzyme activity assays and studies on glycosaminoglycan biosynthesis .

The recombinant form of B3GAT3 is valuable in research focused on understanding the biosynthesis and function of glycosaminoglycans. It is used in enzyme activity assays to study the enzyme’s specificity and kinetics. Additionally, recombinant B3GAT3 is employed in structural studies to elucidate the enzyme’s active site and binding interactions .