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Golgi-targeted HS3st1 localizes in the Golgi and results in the formation of a single type of AT-binding site and high anti-factor Xa (show F10 Proteins) activity
In this paper a conformational change is described that occurs in heparan sulfate 3-O-sulfotransferase-1 upon binding to heparan sulfate.
the 3-OST-1 enzyme produces the majority of tissue anticoagulant heparan sulfate
Hs3st1(-/-) mice do not show an obvious procoagulant phenotype.
Crystal structure of the binary complex of 3-OST-1 and PAP (show ASAP1 Proteins) provide information essential for understanding the biosynthesis of anticoagulant heparan sulfate and the general mechanism of action of heparan sulfate sulfotransferases.
Heparan sulfate biosynthetic enzymes are key components in generating a myriad of distinct heparan sulfate fine structures that carry out multiple biologic activities. The enzyme encoded by this gene is a member of the heparan sulfate biosynthetic enzyme family. It possesses both heparan sulfate glucosaminyl 3-O-sulfotransferase activity, anticoagulant heparan sulfate conversion activity, and is a rate limiting enzyme for synthesis of anticoagulant heparan. This enzyme is an intraluminal Golgi resident protein.
heparan sulfate 3-O-sulfotransferase
, heparan sulfate 3-O-sulfotransferase-1
, heparan sulfate D-glucosaminyl 3-O-sulfotransferase 1
, heparan sulfate (glucosamine) 3-O-sulfotransferase 1
, heparan sulfate glucosamine 3-O-sulfotransferase 1
, heparan sulfate 3-O-sulfotransferase 1
, heparin-glucosamine 3-O-sulfotransferase