FUT10 Protein, Human (HEK293, His)

The FUT10 protein plays a key role in glycosylation, primarily fucosylating the innermost GlcNAc residues in biantennary N-glycans. This activity generates a core α(1->3)-fucose epitope that serves as a recognition signal for targeted degradation of misfolded glycoproteins. FUT10 Protein, Human (HEK293, His) is the recombinant human-derived FUT10 protein, expressed by HEK293 , with N-His labeled tag.

The FUT10 protein takes center stage in glycosylation processes by predominantly fucosylating the innermost N-acetyl glucosamine (GlcNAc) residue in biantennary N-glycan acceptors. This enzymatic activity is postulated to yield the core alpha(1->3)-fucose epitope within the chitobiose unit of biantennary N-glycans, serving as a recognition signal for the targeted degradation of aberrantly folded glycoproteins. Additionally, FUT10 plays a crucial role in the biosynthesis of Lewis X-carrying biantennary N-glycans, contributing to the regulation of neuron stem cell self-renewal during brain development. The enzyme catalyzes the transfer of the fucosyl moiety from GDP-beta-L-fucose to the innermost GlcNAc residue in biantennary N-glycan acceptors, while notably avoiding fucosylation of GlcNAc within the type 2 lactosamine unit.

Human

HEK293

N-His

Q6P4F1-1 (L32-D479)

84750  [NCBI]

Lumenal Domain

LGKFERKEFKSSSLQDGHTKMEEAPTHLNSFLKKEGLTFNRKRKWELDSYPIMLWWSPLTGETGRLGQCGADACFFTINRTYLHHHMTKAFLFYGTDFNIDSLPLPRKAHHDWAVFHEESPKNNYKLFHKPVITLFNYTATFSRHSHLPLTTQYLESIEVLKSLRYLVPLQSKNKLRKRLAPLVYVQSDCDPPSDRDSYVRELMTYIEVDSYGECLRNKDLPQQLKNPASMDADGFYRIIAQYKFILAFENAVCDDYITEKFWRPLKLGVVPVYYGSPSITDWLPSNKSAILVSEFSHPRELASYIRRLDSDDRLYEAYVEWKLKGEISNQRLLTALRERKWGVQDVNQDNYIDAFECMVCTKVWANIRLQEKGLPPKRWEAEDTHLSCPEPTVFAFSPLRTPPLSSLREMWISSFEQSKKEAQALRWLVDRNQNFSSQEFWGLVFKD

Approximately 55-65 kDa,based on SDS-PAGE under reducing conditions,due to the glycosylation.

≥ 95%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.