Recombinant Human B3GAT1 (N-6His)

B3GAT1

Q9P2W7

B3GAT1 is the key enzyme during the biosynthesis of the carbohydrate epitope HNK-1, which is present on a number of cell adhesion molecules important in neurodevelopment. It adds a glucuronic residue to the terminal lactosamine residue (Gal beta 14GlcNAc) of a glycoprotein or glycolipid, which can be further sulfated to become the HNK1 epitope, a unique trisaccharide structure, HSO3-3GlcA beta 1-3Gal beta 1-4GlcNAc. The enzyme activity was found to be enhanced in the presence of sphingomyelin and phosphatidylinositol. The HNK1 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. 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.

36.2 kDa

< 1.0 EU per ug of the protein as determined by the LAL method.

HEK293 Cells

Lyophilized from a 0.2 um filtered solution of 20mM Tris-HCl, 150mM NaCl, pH 8.0.
Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the printed manual.

N-6His

50-60 kDa

> 95 % as determined by reducing SDS-PAGE.

His25-Ile334

B3GAT1;Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1;beta-1;3-glucuronyltransferase 1 (glucuronosyltransferase P);CD57;GlcAT-P;HNK1;NK1;NK-1

Q9P2W7