>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.
45 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.
The CHST family is comprised of 14 enzymes in humans. All members of this family are Golgi-localized type II membrane proteins. Only the luminal and enzymatic domain is expressed in each of our recombinant CHST proteins. These enzymes transfer sulfate (i.e., sulfonate) onto the 6-O or 4-O positions of GalNAc, Gal and GlcNAc residues on glycoproteins, proteoglycans and glycolipids (1). This sulfation often creates specific epitopes that can be recognized by extracellular matrix proteins, cell surface receptors and viruses (2). CHST1, also known as keratan sulfate Gal-6 sulfotransferase, transfers sulfate to position 6 of galactose residues on keratan sulfate (3). It also has sulfotransferase activity on sialyl N-acetyllactosamine structures and participates in biosynthesis of selectin ligands that play a central role in lymphocyte homing at sites of inflammation (4). Human CHST1 shares 94% amino acid sequence identity with mouse CHST1.
The activity of the
recombinant human CHST1 is measured using a PAP-specific phosphatase-coupled
sulfotransferase assay (5).
Hemmerich, S. and S.D. Rosen (2000) Glycobiology 10:849.
Bowman, K.G. and C.R. Bertozzi (1999) Chem. Biol. 5:447.
Fukuta, M. et al. (1997) J. Biol. Chem. 272:32321.
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