>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
<1.0 EU per 1 μg of the protein by the LAL method.
93 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Heparan sulfate is a highly sulfated polysaccharide that can be found on the cell surface and within extracellular matrix. It is typically covalently attached to the protein core of proteoglycans, such as syndecans and glypicans (1, 2). Heparin, on the other hand, is a highly sulfated version of heparan sulfate with no protein core and is predominantly found in mast cells. Both heparin and heparan sulfate contain disaccharide repeats of uronic acid and N‑acetylglucosamine and are modified by the same sulfotransferases (1, 2). The uronic acid residues can be sulfated at the 2-O position by heparan sulfate 2-O sulfotransferase (HS2ST). The N‑acetylglucosamine residues can be sulfated at the N, 3-O, and 6-O positions by N-deacetylase/N-sulfotransferases (NDSTs), heparan sulfate 3‑O sulfotransferases and heparan sulfate 6‑O sulfotransferases, respectively. All these enzymes are Golgi resident proteins. NDST-mediated modifications are believed to occur before modifications by other sulfotransferases (3). There are four NDSTs in the human genome and all are dual enzymes with both deacetylase and sulfotransferase domains (4, 5). NDST1 has both strong deacetylase and sulfotransferase activities. NDST1 deficiency causes developmental defects such as cerebral hypoplasia and craniofacial defects (6). The activity of this recombinant NDST1 is determined using a phosphatase coupled assay (7).
Bernfield, M. et al. (1999) Annu. Rev. Biochem. 68:729.
Esko, J. D. and Selleck, S. B. (2002) Annu. Rev. Biochem. 71:435.
Carlsson, P. et al. (2008) J. Biol. Chem. 283:20008.
Aikawa, J. and Esko, J. D. (1999) J. Biol. Chem. 274:2690.
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