Human Carbohydrate Sulfotransferase 4/
CHST4 Biotinylated Antibody
Human Carbohydrate Sulfotransferase 4/
CHST4 Biotinylated Antibody Summary
aa 23-286
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Reconstitution Calculator
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: Carbohydrate Sulfotransferase 4/CHST4
The CHST family is comprised of 14 enzymes in human. All members of this family are Golgi-localized type II membrane proteins (1). 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 (2). This sulfation often creates specific epitopes that can be recognized by extracellular matrix proteins, cell surface receptors and viruses (3). CHST4, also known as high endothelial cells N-acetylglucosamine 6-O-sulfotransferase (HEC-GlcNAc6ST) or L‑selectin ligand sulfotransferases (LSST), catalyzes the transfer of sulfate to position 6 of non-reducing GlcNAc residues within mucin-associated glycans that ultimately serve as L‑selectin ligands (4). It has a catalytic preference for core 2-branched mucin-type O‑glycans, but also has activity toward core 3 type of O‑glycan (5). Human CHST4 shares 72% amino acid sequence identity with the mouse ortholog.
- deGraffenried, D. and Bertozzi, C.R. (2003) J. Biol. Chem. 278:40282.
- Hemmerich, S. and Rosen, S. (2000) Glycobiology 10:849.
- Bowman, K. G. and Bertozzi, C. R. (1999) Chem. Biol. 5:447.
- Bistrup, A. et al. (1999) J. Cell Biol. 145:899.
- Uchimura, K. et al. (2002) J. Biol. Chem. 277:3979.
- Robbins, P.W. (1962) Methods in Enzymology, Vol. V, Academic Press, Inc., New York, 964.
- MacRae, I.J. I.H. Segel, and A.J. Fisher. (2000) Biochemistry. 39:1613.
- Wu, Z.L. et al. (2002) Faseb J. 16:539.
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