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

HEK293 Cells

His25-Ile334

Q9P2W7

Human

36.2 kDa

50-60 kDa

N-His

Not validated for activity

> 95 % as determined by reducing SDS-PAGE.

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

Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

This product is provided as lyophilized powder which is shipped with ice packs.

Lyophilized from a 0.2 μm filtered solution of 20mM Citrate, 8% Sucrose, 100mM NaCl, 0.05% Tween 80, pH 6.0.
Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the printed manual.

Please refer to the printed manual for detailed information.

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.