HS3ST1 Protein, Human (sf9, His)

The HS3ST1 protein utilizes PAPS to crucially catalyze the transfer of sulfate to position 3 of the glucosamine residue in heparan sulfate (HS), representing the rate-limiting step in HS biosynthesis. This activity is essential for the formation of the anticoagulant heparan sulfate and completion of the antithrombin pentasaccharide binding site. HS3ST1 Protein, Human (sf9, His) is the recombinant human-derived HS3ST1 protein, expressed by Sf9 insect cells , with N-His labeled tag. The total length of HS3ST1 Protein, Human (sf9, His) is 287 a.a., with molecular weight of ~36 KDa.

HS3ST1 protein, a sulfotransferase utilizing 3'-phospho-5'-adenylyl sulfate (PAPS) as its substrate, plays a pivotal role in the biosynthesis of heparan sulfate (HS) by catalyzing the transfer of a sulfo group to position 3 of glucosamine residues in heparan. This enzymatic activity represents the rate-limiting step in HS biosynthesis, crucial for the formation of anticoagulant heparan sulfate. The sulfation at position 3 of glucosamine residues, facilitated by HS3ST1, is particularly significant as it completes the structure of the antithrombin pentasaccharide binding site. By modulating heparan sulfate biosynthesis, HS3ST1 contributes to the generation of structurally specific molecules involved in anticoagulation, emphasizing its crucial role in regulating blood coagulation processes.

Human

Sf9 insect cells

N-His

O14792 (R21-H307)

9957  [NCBI]

Approximately 36 kDa.

Greater than 95% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.