B3GAT3 is an essential enzyme involved in the synthesis of the linkage region of heparan sulfate and chondroitin sulfate proteoglycans. It transfers a glucuronic acid moiety from the uridine diphosphate-glucuronic acid (UDP-GlcA) to the trisaccharide Gal beta 1-3Gal beta 1-4Xyl covalently bound to a Ser residue at the glycosaminylglycan attachment site of proteoglycans. B3GAT3 knockout mice are embryonic lethal before the 8-cell stage due to failed cytokinesis, suggesting critical roles for chondroitin sulfate and heparan sulfate in embryonic cell division. Unlike the broad substrate specificity exhibited by B3GAT1, B3GAT3 shows strict specificity for Gal beta 1-3Gal beta 1. The crystal structure shows the enzyme is an alpha / beta protein with two subdomains that constitute the donor and acceptor binding sites with the active site lying in the cleft between the two subdomains. Like most known glycosyltransferases, B3GAT3 is a type II Golgi-resident transmembrane protein with a short N‑terminal cytoplasmic domain and a single-pass transmembrane domain followed by an enzymatic domain in the lumen of Golgi apparatus. In the current assay, hydrolase activity against UDP-GlcA was measured using a phosphatase-coupled method.
Post-translational: N-glycosylated.
生物活性
Measured by its ability to hydrolyze UDP-GlcA. The specific activity is >1 pmol/min/μg, as measured under the described conditions.
Store at -20°C for 1 year. Avoid freeze/thaw cycle.
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Recombinant Human B3GAT3 Protein (rp183658) - SDS-PAGE 3 μg/lane of Recombinant Human B3GAT3 Protein was resolved with SDS-PAGE under reducing (R) and non-reducing (N) conditions and visualized by Coomassie® Blue staining, showing a band at 31.2 & 63.4 kDa.
ZJ24F1215628
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