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Recombinant Human ST8SIA1 Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 6716-GT

R&D Systems, part of Bio-Techne
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6716-GT-020

Key Product Details

Source

CHO

Accession #

Conjugate

Unconjugated

Applications

Enzyme Activity

Product Specifications

Source

Chinese Hamster Ovary cell line, CHO-derived human ST8 alpha-2,8-Sialyltransferase 8A/ST8SIA1 protein
Tyr49-Ser356, with a C-terminal 6‑His tag

Purity

>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain at 5 μg per lane.

Endotoxin Level

<1.0 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Tyr49

Predicted Molecular Mass

36 kDa

SDS-PAGE

40-60 kDa, reducing conditions

Activity

Measured by its ability to transfer Neu5Ac from CMP-Neu5Ac to fetuin of fetal calf serum.
The specific activity is >15 pmol/min/μg, as measured under the described conditions.

Formulation, Preparation and Storage

6716-GT
Formulation Supplied as a 0.2 μm filtered solution in Tris and NaCl.
Shipping The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -70 °C as supplied.
  • 3 months, -70 °C under sterile conditions after opening.

Background: ST8 alpha-2,8-Sialyltransferase 8A/ST8SIA1

Gangliosides are acidic glycosphingolipids that contain one or more sialic acid residues and are particularly prevalent on neuronal cells (1). Ganglioside GD3 is involved in cell adhesion and the growth of cultured malignant cells (2). ST8SIA1 is a sialyltransferase that catalyzes the transfer of sialic acid from CMP-sialic acid to GM3 (NeuNAc alpha2‑3Gal beta1‑4Glc‑Cer) to produce GD3 (NeuNAc alpha2‑8NeuNAc alpha2‑3Gal beta1‑4Glc‑Cer) and GT3 (NeuNAc alpha2‑8NeuNAc alpha2‑8NeuNAc alpha2‑3Gal beta1‑4Glc‑Cer) in a successive manner (3); therefore the enzyme has both GD3 and GT3 synthase activity (4). ST8SIA1 is mainly expressed in adult and fetal brain, and its expression is enhanced in melanoma cell lines (3, 4, 5). Like most known glycosyltransferases, ST8SIA1 is predicted as a type II transmembrane protein with a short N‑terminal cytoplasmic domain and a single-pass transmembrane domain followed by an enzymatic domain in the lumen of the Golgi apparatus. However, recently GD3 synthase activity was demonstrated at the surface of epithelial and melanoma cells, suggesting glycosphingolipid synthesis may occur at the cell membrane (6). Recombinant ST8SIA1 also showed activity on fetuin from fetal calf serum, when measured using a phosphatase-coupled method (7).

References

  1. Kolter, T. et al. (2002) J. Biol. Chem. 277:25859.
  2. Cheresh, D.A. et al. (1986) J. Cell. Biol. 102:688.
  3. Nakayama, J. et al. (1986) J. Biol. Chem. 271:3684.
  4. Nara, K. et al. (1994) Proc. Natl. Acad. Sci. USA. 91:7952.
  5. Haraguchi, M. et al. (1994) Proc. Natl. Acad. Sci. USA. 91:10455.
  6. Crespo, P.M. et al. (2010) J. Biol. Chem. 285:29179.
  7. Wu, Z.L. et al. (2010) Glycobiology doi: 10.1093/glycob/cwq187.

Long Name

ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 1

Alternate Names

GD3S, SIAT8A, ST8SiaI

Entrez Gene IDs

6489 (Human); 20449 (Mouse); 25280 (Rat)

Gene Symbol

ST8SIA1

UniProt

Additional ST8 alpha-2,8-Sialyltransferase 8A/ST8SIA1 Products

Product Documents for Recombinant Human ST8SIA1 Protein, CF

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot number in the search box below.

Note: Certificate of Analysis not available for kit components.

Product Specific Notices for Recombinant Human ST8SIA1 Protein, CF

For research use only

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