beta ‑1,3-Glucuronyltransferase 1/B3GAT1 in Rat Cortical Stem Cells. |
beta ‑1,3-Glucuronyltransferase 1/B3GAT1 was detected in immersion fixed differentiated rat cortical stem cells using Mouse Anti-Rat beta ‑1,3-Glucuronyltransferase 1/B3GAT1 Monoclonal Antibody (Catalog # MAB6698) at 10 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Mouse IgG Secondary Antibody (red; Catalog # NL007). Oligo2 was also detected in the cells using Human Olig2 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF2418) and NorthernLights™ 637-conjugated Anti-Goat IgG Secondary Antibody (green; Catalog # NL003). Cells were counterstained with DAPI (blue). Specific staining of B3GAT1 was localized to transmembrane Golgi. View our protocol for Fluorescent ICC Staining of Stem Cells on Coverslips.
B3GAT1 is a key enzyme involved in human natural killer-1 (HNK-1) epitope synthesis. It adds a glucuronic residue to the terminal lactosamine residue (Gal beta 1-4GlcNAc-) of a glycoprotein or glycolipid, which can be further sulfated to become the HNK-1 epitope, a unique trisaccharide structure, HSO3-3GlcA beta 1-3Gal beta 1-4GlcNAc- (1, 2). The enzyme activity was found to be enhanced in the presence of sphingomyelin and phosphatidylinositol (3).The HNK-1 carbohydrate epitope is characteristically expressed on a series of cell adhesion molecules in addition to some glycolipids in the extracellular matrix and on the cell surface in the nervous system, where it is involved in cell‑cell and cell‑substratum interaction and recognition during the development of the nervous system (4). Like most known glycosyltransferases, B3GAT1 is a type II Golgi-resident transmembrane protein with a short N‑terminal cytoplasmic domain and a single‑pass transmembrane domain followed by an enzymatic domain in the lumen of Golgi apparatus. The enzyme activity was assayed using a phosphatase-coupled method (5).
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