Recombinant Human B3GNT2 Protein (Fc Tag) | PKSH031125

(No reviews yet) Write a Review
SKU:
575-PKSH031125
€998.00
Frequently bought together:

Description

Recombinant Human B3GNT2 Protein (Fc Tag) | PKSH031125 | Gentaur US, UK & Europe Disrtribition

Synonyms: B3GN-T2;B3GNT;B3GNT-2;B3GNT1;BETA3GNT;BGnT-2;BGNT2

Active Protein: N/A

Activity: A DNA sequence encoding the human B3GNT2 (Q9NY97-1) (Lys29-Cys397) was expressed, with the fused Fc region of human IgG1 at the N-terminus.

Protein Construction: A DNA sequence encoding the human B3GNT2 (Q9NY97-1) (Lys29-Cys397) was expressed, with the fused Fc region of human IgG1 at the N-terminus.

Fusion Tag: N-Fc

Species: Human

Expressed Host: HEK293 Cells

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

Purity: > 90 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per µg as determined by the LAL method.

Stability and Storage: 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.

Molecular Mass: 71.2 kDa

Formulation: Lyophilized from sterile PBS, pH 7.4

Reconstitution: Please refer to the printed manual for detailed information.

Background: B3GNT2 belongs to the beta-1, 3-N-acetylglucosaminyltransferase family. It is a type II transmembrane protein which prefers the substrate of lacto-N-neotetraose. Alternative splicing produced 2 isoforms of the human protein. B3GNT2 catalyzes the initiation and elongation of poly-N- acetyllactosamine chains. Enzymatic activities of some glycosyltransferases are markedly increased via complex formation with other transferases or cofactor proteins. B3GNT2 and beta3Gn-T8 can form a heterodimer in vitro and that the complex exhibits much higher enzymatic activity than either enzyme alone. It is found that up-regulation of beta3Gn-T8 in differentiated HL-60 cells may increases poly-N-acetyllactosamine chains by activating intrinsic B3GNT2.

Research Area: N/A

View AllClose