FUT8 Protein, Human (sf9, His)

The FUT8 protein acts as a catalyst during glycosylation, specifically adding fucose in an α1-6 linkage to the first GlcNAc residue located near the N-glycan peptide chain. This enzymatic activity plays a crucial role in glycoprotein modification, contributing to the structural diversity and functional properties of N-glycans. FUT8 Protein, Human (sf9, His) is the recombinant human-derived FUT8 protein, expressed by Sf9 insect cells , with C-His labeled tag.

FUT8, or alpha-1,6-fucosyltransferase 8, is an enzyme that plays a key role in glycosylation processes by catalyzing the addition of fucose in an alpha 1-6 linkage to the initial GlcNAc residue adjacent to peptide chains in N-glycans. This enzymatic activity is crucial for the modification of glycoproteins, influencing their structure and function. By specifically adding fucose in this alpha 1-6 linkage, FUT8 contributes to the diverse repertoire of glycan structures, impacting cellular recognition, signaling, and other essential biological processes. It has to highlight FUT8's specificity in glycan modification, shedding light on its role in shaping the glycoproteome and participating in various cellular functions influenced by glycosylation.

Measured by its ability to hydrolyze the donor substrate GDP fucose and the specific activity is >0.75 pmoles/min/μg.

Human

Sf9 insect cells

C-His

Q9BYC5-1 (R68-K575)

2530  [NCBI]

Approximately 55 kDa

Greater than 95% as determined by reducing SDS-PAGE.

Solution.

Supplied as a 0.2 μm filtered solution of 20 mM Tris, 500 mM NaCl, pH 8.0, 10% gly.

<1 EU/μg, determined by LAL method.

N/A.

Stored at -80°C for 1 year. It is stable at -20°C for 3 months after opening. It is recommended to freeze aliquots at -80°C for extended storage. Avoid repeated freeze-thaw cycles.

Shipping with dry ice.