|Other Names||Carbohydrate sulfotransferase 2, 282-, Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 2, GST-2, N-acetylglucosamine 6-O-sulfotransferase 1, GlcNAc6ST-1, Gn6ST-1, CHST2, GN6ST|
|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||Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues within keratan-like structures on N-linked glycans and within mucin-associated glycans that can ultimately serve as SELL ligands. SELL ligands are present in high endothelial cells (HEVs) and play a central role in lymphocyte homing at sites of inflammation. Participates in biosynthesis of the SELL ligand sialyl 6-sulfo Lewis X and in lymphocyte homing to Peyer patches. Has no activity toward O-linked sugars. Its substrate specificity may be influenced by its subcellular location. Sulfates GlcNAc residues at terminal, non-reducing ends of oligosaccharide chains.|
|Cellular Location||Golgi apparatus, trans-Golgi network membrane; Single-pass type II membrane protein|
|Tissue Location||Widely expressed. Highly expressed in bone marrow, peripheral blood leukocytes, spleen, brain, spinal cord, ovary and placenta. Expressed by high endothelial cells (HEVs) and leukocytes.|
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Provided below are standard protocols that you may find useful for product applications.
N-acetylglucosamine-6-O-sulfotransferases, such as CHST2,catalyze the transfer of sulfate from 3-prime-phosphoadenosine5-prime-phosphosulfate (PAPS) to position 6 of a nonreducingN-acetylglucosamine (GlcNAc) residue (Uchimura et al., 1998 [PubMed9722682]).
Shimada, M., et al. Hum. Genet. 128(4):433-441(2010)Ross, C.J., et al. Nat. Genet. 41(12):1345-1349(2009)Desko, M.M., et al. Glycobiology 19(10):1068-1077(2009)Saito, A., et al. J. Hum. Genet. 54(6):317-323(2009)Kanoh, A., et al. Glycoconj. J. 23 (5-6), 453-460 (2006) :
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