Detection of Human Carbohydrate Sulfotransferase 1/CHST1 by Western Blot. |
Western blot shows lysates of human tonsil tissue. PVDF membrane was probed with 1 µg/mL of Sheep Anti-Human Carbohydrate Sulfotransferase 1/CHST1 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF5316) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for Carbohydrate Sulfotransferase 1/CHST1 at approximately 48 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 8.
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.
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