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Highly-purified recombinant NDST-4 and a selective library of structurally-defined oligosaccharides were employed to determine the substrate specificity of rNDST-4. Full-length rNDST-4 lacks obvious N-deacetylase activity, and displays only N-sulfotransferase activity. NDST-4 did not show directional N-sulfotransferase activity while the N-deacetylase domain was inactive.
The rs12108602 near NDST4 showed significant associations with MaxDrinks.
NDST4 gene is a novel candidate tumor suppressor gene in human cancer.
Our results suggest that genetic variants in TYW3/CRYZ and NDST4 loci may be involved in the regulation of circulating resistin levels
this study revealed the involvement of Ndst4 in the development and homeostasis of colonic epithelium
Essential bifunctional enzyme that catalyzes both the N- deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA dissacharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis. Has low deacetylase activity but high sulfotransferase activity.
, N-heparan sulfate sulfotransferase 4
, bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 4
, glucosaminyl N-deacetylase/N-sulfotransferase 4
, N-deacetylase/N-sulfotransferase (heparin glucosaminyl) 4
, N-deacetylase/N-sulfotransferase 4