UAP1 Protein, Human (P.pastoris, His)

UAP1 protein functions as an enzyme that catalyzes the conversion of UTP and GlcNAc-1-P into UDP-GlcNAc, as well as UTP and GalNAc-1-P into UDP-GalNAc. Notably, isoform AGX1 exhibits 2 to 3 times higher activity towards GalNAc-1-P, while isoform AGX2 displays 8 times more activity towards GlcNAc-1-P, highlighting distinct substrate preferences between the isoforms. UAP1 Protein, Human (P.pastoris, His) is the recombinant human-derived UAP1 protein, expressed by P. pastoris , with N-His labeled tag. The total length of UAP1 Protein, Human (P.pastoris, His) is 522 a.a., with molecular weight of ~60.8 kDa.

Uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) and uridine diphosphate-N-acetylgalactosamine (UDP-GalNAc) are crucial nucleotide sugars involved in glycosylation processes, and the UAP1 protein plays a central role in their synthesis. UAP1 converts uridine triphosphate (UTP) in conjunction with either GlcNAc-1-P or GalNAc-1-P to generate UDP-GlcNAc or UDP-GalNAc, respectively. Interestingly, isoform AGX1 of UAP1 exhibits 2 to 3 times higher activity towards GalNAc-1-P, emphasizing its preference for galactosamine, while isoform AGX2 displays 8 times greater activity towards GlcNAc-1-P, highlighting its specificity for N-acetylglucosamine. The differential activities of these isoforms underscore the versatility of UAP1 in contributing to the generation of distinct nucleotide sugars, crucial for various glycosylation events in cellular processes.

Human

P. pastoris

N-His

Q16222 (1M-522I)

6675  [NCBI]

MNINDLKLTLSKAGQEHLLRFWNELEEAQQVELYAELQAMNFEELNFFFQKAIEGFNQSSHQKNVDARMEPVPREVLGSATRDQDQLQAWESEGLFQISQNKVAVLLLAGGQGTRLGVAYPKGMYDVGLPSRKTLFQIQAERILKLQQVAEKYYGNKCIIPWYIMTSGRTMESTKEFFTKHKYFGLKKENVIFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQRGIWSIHVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEISLATAQKRSSDGRLLFNAGNIANHFFTVPFLRDVVNVYEPQLQHHVAQKKIPYVDTQGQLIKPDKPNGIKMEKFVFDIFQFAKKFVVYEVLREDEFSPLKNADSQNGKDNPTTARHALMSLHHCWVLNAGGHFIDENGSRLPAIPRSATNGKSETITADVNHNLKDANDVPIQCEISPLISYAGEGLESYVADKEFHAPLIIDENGVHELVKNGI

Approximately 60.8 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.