Galectin-8/LGALS8 Protein, Human (GST)

Galectin-8/LGALS8 Protein, a vital enzyme in glycosylation, serves as a beta-1,3-N-acetylglucosaminyltransferase, synthesizing poly-N-acetyllactosamine. Crucial for modifying glycoproteins and glycolipids, Galectin-8/LGALS8 catalyzes N-acetylglucosamine transfer onto acceptor molecules, exhibiting specific activity for type 2 oligosaccharides. Its role in poly-N-acetyllactosamine synthesis emphasizes its significance in modulating cellular interactions, impacting various processes like cell adhesion, signaling, and recognition events through glycan structure alterations. Galectin-8/LGALS8 Protein, Human (GST) is the recombinant human-derived Galectin-8/LGALS8 protein, expressed by E. coli, with N-GST labeled tag. The total length of Galectin-8/LGALS8 Protein, Human (GST) is 317 a.a., with molecular weight of 62.8 kDa.

B3GNT4, a key enzyme in glycosylation processes, functions as a beta-1,3-N-acetylglucosaminyltransferase responsible for synthesizing poly-N-acetyllactosamine. This enzyme plays a crucial role in the modification of glycoproteins and glycolipids by catalyzing the transfer of N-acetylglucosamine residues onto acceptor molecules. Notably, B3GNT4 exhibits specific activity for type 2 oligosaccharides, contributing to the diversification and complexity of glycan structures. The synthesis of poly-N-acetyllactosamine by B3GNT4 underscores its significance in modulating cellular interactions, as alterations in glycan structures can impact various biological processes, including cell adhesion, signaling, and recognition events.

Human

E. coli

N-GST

O00214 (M1-W317)

3964  [NCBI]

MMLSLNNLQNIIYNPVIPFVGTIPDQLDPGTLIVIRGHVPSDADRFQVDLQNGSSMKPRADVAFHFNPRFKRAGCIVCNTLINEKWGREEITYDTPFKREKSFEIVIMVLKDKFQVAVNGKHTLLYGHRIGPEKIDTLGIYGKVNIHSIGFSFSSDLQSTQASSLELTEISRENVPKSGTPQLRLPFAARLNTPMGPGRTVVVKGEVNANAKSFNVDLLAGKSKDIALHLNPRLNIKAFVRNSFLQESWGEEERNITSFPFSPGMYFEMIIYCDVREFKVAVNGVHSLEYKHRFKELSSIDTLEINGDIHLLEVRSW

62.8 kDa

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

<1 EU/μg, determined by LAL method.