Recombinant Human ST6GalNAc1 (alpha-N-acetylgalactosaminide α-2,6-sialyltransferase 1), soluble fragment
Alpha-N-acetylgalactosaminide α-2,6-sialyltransferase 1 catalyzes the transfer of sialic acid N-acetylneuraminic acid (Neu5Ac) from cytidine 5'-monophosphono-N-acetylneuraminic acid (CMP-Neu5Ac) to O-linked GalNAc residues in an α-2,6 linkage (1). ST6GalNAcI belongs to a large family of Golgi-membrane-bound sialyltransferases that is responsible for the biosynthesis of sialyated structures, and from which approximately 20 have been cloned to date (2). The cancer associated sialyl-Tn (sTn) angtigen is formed by ST6GalNAcI, through the transfer of Neu5Ac to GalNAc resiudes on mucins (1,3,4). Addition of a sialic acid to a glyco-protein effectively caps the glycan-chain, preventing further additions (5). The presence of sialic acid residues extends the half-life of circulating proteins, and are considered to be important for a large variety of biotherapuetics (6).
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- Harduin-Lepers, A. et al. (2001) Biochimie 83, 727.
- Marcos, N.T. et al. (2004) Cancer Res. 64, 7050.
- Sewell, R. et al. (2006) J. Biol. Chem. 281, 3586.
- Gill, D.J. et al. (2011) Trends Cell Biol. 21, 149.
- Varki, A. (2008) Trends Mol. Med. 14, 351.
Catalog #: SBH-003-ST6GalNAc1
Source : Insect Cells, Accession # Q9NSC7
Formulation: Sterile filtered solution in 20mM Hepes pH7 and 100mM NaCl, at a stock concentration of 500 ug/mL.
Stability: Stable for 4 weeks at 4C. Stable for 6 months at -80C. Avoid repeated freeze-thaw cycles.
Purity: Greater than 90% by SDS-PAGE.
Biological Activity: Measured by transfer of NeuAc from CMP-NeuAc to the Tn-peptide MEELGMAPALQPT(GalNAc)QGAMPAF, enzyme reactions containing: 25mM MES pH 6.5, 20mM EDTA, 1mM DTT, 2mM CMP-NeuAc and 10μg (400ug/mL final) Tn-peptide. Final reaction contained 175ng of ST6GalNAcI. Incubated at 37ºC. Specific activity > 50 pmol/min/μg.
PubMed Link: ST6GalNAc1 Human
Usage: For research only. Not for use in diagnostic or therapeutic procedures.
Country of Origin: USA