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The persistence of a latent hexamer-building interface in the human enzyme suggests that the ancestral UXS may have been a hexamer.
hUXS forms a tetramer in solution that is important for activity. The higher activity of the tetramer coupled with the relative instability of the dimeric complex suggests that an association-dissociation mechanism may regulate hUXS activity.
UDP-glucuronate decarboxylase, a key enzyme in proteoglycan synthesis: cloning, characterization, and localization.
Complementation was achieved by expression of a cytoplasmic variant of UDP-xylose Synthase, which proves the existence of a functional Golgi UDP-xylose transporter[UDP-xylose Synthase]
analysis of chondroitin sulfate and heparan sulfate biosynthesis in zebrafish larvae homozygous for mutations in ext2, extl3, uxs1, or b3gat3
These results show that uxs1 transcript is localized in a pattern consistent with the mutant craniofacial phenotype, and that transcript instability may contribute to the loss of uxs1 function in uxs1hi3357 larvae.
This gene encodes an enyzme found in the perinuclear Golgi which catalyzes the synthesis of UDP-xylose used in glycosaminoglycan (GAG) synthesis on proteoglycans. The GAG chains are covalently attached to proteoglycans which participate in signaling pathways during development. Multiple transcript variants encoding different isoforms have been found for this gene.
UDP-glucuronic acid decarboxylase 1
, UDP-glucuronate decarboxylase 1
, short chain dehydrogenase/reductase family 6E, member 12