|Other Names||Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 3, Glucosaminyl N-deacetylase/N-sulfotransferase 3, NDST-3, hNDST-3, N-heparan sulfate sulfotransferase 3, N-HSST 3, Heparan sulfate N-deacetylase 3, 3---, Heparan sulfate N-sulfotransferase 3, 282-, NDST3, HSST3|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||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 disaccharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis. Has high deacetylase activity but low sulfotransferase activity.|
|Cellular Location||Golgi apparatus membrane; Single-pass type II membrane protein|
|Tissue Location||Expressed in brain, kidney, liver, fetal and adult lung, adult pancreas, placenta, fetal spleen and fetal thymus. Not detected in adult/ fetal heart and skeletal muscle|
email@example.com, and receive a free "I Love Antibodies" mug.
Provided below are standard protocols that you may find useful for product applications.
This gene encodes a member of the heparan sulfate/heparinGlcNAc N-deacetylase/ N-sulfotransferase family. The encoded enzymeis a type II transmembrane protein that resides in the Golgiapparatus. This monomeric bifunctional enzyme catalyzes theN-deacetylation and N-sulfation of N-acetylglucosamine residues inheparan sulfate and heparin, which are the initial chemicalmodifications required for the biosynthesis of the functionaloligosaccharide sequences that define the specific ligand bindingactivities of heparan sulfate and heparin.
Feng, T., et al. Hum. Genet. 128(3):269-280(2010)Rose, J.E., et al. Mol. Med. 16 (7-8), 247-253 (2010) :Kalsi, G., et al. Hum. Mol. Genet. 19(12):2497-2506(2010)Krenn, E.C., et al. Biochem. Biophys. Res. Commun. 375(3):297-302(2008)Grobe, K., et al. Biochim. Biophys. Acta 1573(3):209-215(2002)
If you have any additional inquiries please email technical services at firstname.lastname@example.org.