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Recombinant Mouse ST6GALNAC2 Protein, CF

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Product Details

Summary
Reactivity MuSpecies Glossary
Applications Enzyme Activity
Format
Carrier-Free

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Recombinant Mouse ST6GALNAC2 Protein, CF Summary

Details of Functionality
Measured by its ability to transfer Neu5Ac from CMP-Neu5Ac to fetuin of fetal calf serum.<br />The specific activity is &gt;700 pmol/min/μg, as measured under the described conditions. <br /><br />
Accession #
N-terminal Sequence
Ser28
Protein/Peptide Type
Recombinant Enzymes
Endotoxin Note
<1.000 EU per 1 µg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Enzyme Activity
Theoretical MW
40 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.
SDS-PAGE
40-50 kDa, reducing conditions
Publications
Read Publication using
6468-GT in the following applications:

Packaging, Storage & Formulations

Storage
Store the unopened product at -70 °C. Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Do not use past expiration date.
Buffer
Supplied as a 0.2 μm filtered solution in Tris and NaCl.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse ST6GALNAC2 Protein, CF

  • (alpha-N-acetylneuraminyl-2,3-beta-galactosyl-1,3)-N-acetyl galactosaminide B
  • alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2
  • EC 2.4.99.-
  • FLJ45660
  • GalNAc alpha-2,6-sialyltransferase II
  • SAITL1
  • sialyltransferase 7((alpha-N-acetylneuraminyl-2,3-beta-galactosyl-1,3)-N-acetyl galactosaminide B
  • sialyltransferase 7((alpha-N-acetylneuraminyl-2,3-beta-galactosyl-1,3)-N-acetyl galactosaminidealpha-2,6-sialyltransferase) B
  • sialyltransferase 7((alpha-N-acetylneuraminyl-2,3-beta-galactosyl-1,3)-N-acetyl galactosaminidealpha-2,6-sialyltransferase)
  • Sialyltransferase 7B
  • sialyltransferase-like 1
  • SIAT7
  • SIAT7B
  • SIAT7-B
  • SIATL1
  • ST6 (alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3)-N-acetylgalactosaminidealpha-2,6-sialyltransferase 2
  • ST6GalNAc II
  • ST6GALNAC2
  • ST6GalNAcII
  • ST6GalNAII
  • STHM
  • STHM(alpha-N-acetylneuraminyl-2,3-beta-galactosyl-1,3)-N-acetyl galactosaminidealpha-2,6-sialyltransferase

Background

Sialic acid molecules attached to glycoproteins or glycosphingolipids play important roles in various biological processes such as immune recognition, pathogen infection, and cell adhesion. Sialyltransferases are key enzymes that regulate the serum levels of sialic acid‑containing molecules. Alpha‑N‑acetylgalactosaminide alpha ‑2,6‑sialyltransferase 2, encoded by the ST6GALNAC2 gene, is a type II membrane protein localized in the Golgi network and catalyzes 2,6‑sialylation of the Tn antigen (GalNAc‑O‑Ser/Thr) (1). Sialyl‑Tn antigen is highly expressed in several human carcinomas and is associated with carcinoma aggressiveness and poor prognosis. Cells transfected with ST6GALNAC2 synthesized the sialyl‑6T structure [Gal beta 1‑3 (Neu5Ac alpha 2‑6)GalNAc‑O‑Ser/Thr] (2). In vitro analysis revealed that the enzyme can use both Gal beta 1‑3GalNAc and Neu5Ac alpha 2‑3Gal beta 1-3GalNAc  as acceptor substrates (3). Recently, it has been reported that disregulation of this gene is involved in the pathogenesis of IgA nephropathy, a common kidney disease that occurs when antibody IgA accumulates in kidneys (4). The enzyme may also be used to synthesize a cancer vaccine (5, 6). At the protein level, mouse ST6GALNAC2 shows 75% amino acid sequence identity with the human homologue. The activity of this enzyme has been measured using a phosphatase‑coupled assay (7).
  1. Kono, M., et al. (2000) Biochem. Biophys. Res. Commun. 272:94.
  2. Marcos, N.T., et al. (2004) Cancer Res. 64:7050.
  3. Samyn-Petit, B., et al. (2000) Biochim. Biophys. Acta 1474:201.
  4. Li, G.S., et al. (2007) Hum. Mutat. 28:950.
  5. Julien, S., et al. (2009) Br. J. Cancer 100:1746.
  6. Sewell, R., et al. (2006) J. Biol. Chem. 281:3586.
  7. Wu, Z.L., et al. (2011) Glycobiology 21:727.

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Publications for ST6 Sialyltransferase 2/ST6GALNAC2 (6468-GT)(1)

We have publications tested in 1 confirmed species: E. coli.

We have publications tested in 1 application: Bioassay.


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