POMGNT1 Protein, Human (HEK293, His)

The POMGNT1 protein crucially directs O-mannosyl glycosylation, which adds N-acetylglucosamine to O-linked mannose residues on glycoproteins. It catalyzes GlcNAc(beta1-2)Man(alpha1-)O-Ser/Thr on α-dystroglycan and other O-mannosylated proteins, laying the foundation for subsequent carbohydrate addition. POMGNT1 Protein, Human (HEK293, His) is the recombinant human-derived POMGNT1 protein, expressed by HEK293 , with C-6*His labeled tag.

POMGNT1 Protein plays a pivotal role in O-mannosyl glycosylation by facilitating the addition of N-acetylglucosamine to O-linked mannose residues on glycoproteins. Specifically, it catalyzes the synthesis of the GlcNAc(beta1-2)Man(alpha1-)O-Ser/Thr moiety on alpha-dystroglycan and various other O-mannosylated proteins. This enzymatic activity serves as a fundamental step, laying the groundwork for subsequent additions of carbohydrate moieties. Notably, POMGNT1 demonstrates specificity for alpha-linked terminal mannose and lacks activity corresponding to MGAT3, MGAT4, MGAT5, MGAT7, or MGAT8. The intricate glycosylation process orchestrated by POMGNT1 highlights its essential contribution to the structural complexity and functional diversity of glycoproteins.

Human

HEK293

C-6*His

Q8WZA1-1 (L59-T660)

55624  [NCBI]

Lumenal Domain

LDTRRAISEANEDPEPEQDYDEALGRLEPPRRRGSGPRRVLDVEVYSSRSKVYVAVDGTTVLEDEAREQGRGIHVIVLNQATGHVMAKRVFDTYSPHEDEAMVLFLNMVAPGRVLICTVKDEGSFHLKDTAKALLRSLGSQAGPALGWRDTWAFVGRKGGPVFGEKHSKSPALSSWGDPVLLKTDVPLSSAEEAECHWADTELNRRRRRFCSKVEGYGSVCSCKDPTPIEFSPDPLPDNKVLNVPVAVIAGNRPNYLYRMLRSLLSAQGVSPQMITVFIDGYYEEPMDVVALFGLRGIQHTPISIKNARVSQHYKASLTATFNLFPEAKFAVVLEEDLDIAVDFFSFLSQSIHLLEEDDSLYCISAWNDQGYEHTAEDPALLYRVETMPGLGWVLRRSLYKEELEPKWPTPEKLWDWDMWMRMPEQRRGRECIIPDVSRSYHFGIVGLNMNGYFHEAYFKKHKFNTVPGVQLRNVDSLKKEAYEVEVHRLLSEAEVLDHSKNPCEDSFLPDTEGHTYVAFIRMEKDDDFTTWTQLAKCLHIWDLDVRGNHRGLWRLFRKKNHFLMVGVPASPYSVKKPPSVTPIFLEPPPKEEGAPGAPEQT

Approximately 79 kDa,based on SDS-PAGE under reducing conditions.

≥ 90%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.