Cytosolic beta-Glucosidase/GBA3 Protein, Human (GST)

Cytosolic β-glucosidase/GBA3 is a multifunctional neutral cytosolic β-glucosidase that displays broad substrate specificity, suggesting a possible involvement in glycosylceramide catabolism. Although it exhibits significant glucosylceramidase activity in vitro, its in vivo relevance is unclear. Cytosolic beta-Glucosidase/GBA3 Protein, Human (GST) is the recombinant human-derived Cytosolic beta-Glucosidase/GBA3 protein, expressed by E. coli , with N-GST labeled tag.

Cytosolic beta-Glucosidase/GBA3, characterized as a neutral cytosolic beta-glycosidase, exhibits a broad substrate specificity, suggesting potential involvement in the catabolism of glycosylceramides. While demonstrating significant glucosylceramidase activity in vitro, its in vivo relevance remains unclear. The enzyme also hydrolyzes galactosylceramides/GalCers, glucosylsphingosines/GlcSphs, and galactosylsphingosines/GalSphs, although the physiological importance of these activities is not fully elucidated. Furthermore, Cytosolic beta-Glucosidase/GBA3 displays transxylosylase activity in vitro, utilizing xylosylated ceramides/XylCers as donors and cholesterol as an acceptor. Notably, the enzyme exhibits versatility in hydrolyzing various dietary glycosides, including phytoestrogens, flavonols, flavones, flavanones, and cyanogens, suggesting a potential role in xenobiotic metabolism. Additionally, it may contribute to the catabolism of cytosolic sialyl free N-glycans.

Human

E. coli

N-GST

Q9H227-1 (M1-L162)

57733  [NCBI]

MAFPAGFGWAAATAAYQVEGGWDADGKGPCVWDTFTHQGGERVFKNQTGDVACGSYTLWEEDLKCIKQLGLTHYRFSLSWSRLLPDGTTGFINQKAIQLDKVNLQVYCAWSLLDNFEWNQGYSSRFGLFHVDFEDPARPRVPYTSAKEYAKIIRNNGLEAHL

Approximately 45.3 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.