Human ST8 alpha-2,8‑Sialyltransferase 8A/ST8SIA1 Alexa Fluor® 488-conjugated Antibody

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.

Preparation and Storage

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 alpha 2‑3Gal beta 1‑4Glc‑Cer) to produce GD3 (NeuNAc alpha 2‑8NeuNAc alpha 2‑3Gal beta 1‑4Glc‑Cer) and GT3 (NeuNAc alpha 2‑8NeuNAc alpha 2‑8NeuNAc alpha 2‑3Gal beta 1‑4Glc‑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).

Product Datasheets

Related Research Areas

• Glycobiology-related Enzymes
• Search Glycobiology-related Enzymes