ST6GAL1 Human, sf9
Description
Product Specs
Product Science Overview
ST6 Beta-Galactosamide Alpha-2,6-Sialyltransferase 1 (ST6GAL1) is an enzyme that belongs to the glycosyltransferase family 29. This enzyme is responsible for the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates, forming NeuAcα2,6-Gal linkages in N-linked glycans . The recombinant form of this enzyme, expressed in sf9 insect cells, is used for various research and therapeutic purposes.
ST6GAL1 was originally purified from rat liver tissues to homogeneity, which led to the identification of its cDNA . The enzyme was first described as ST6N and later termed Siat1 by the International System for Gene Nomenclature . The human recombinant form of ST6GAL1 is expressed in sf9 insect cells, which are derived from the fall armyworm Spodoptera frugiperda. This expression system is widely used for producing recombinant proteins due to its high yield and proper post-translational modifications.
ST6GAL1 is a type II membrane protein with a calculated molecular mass of approximately 43.5 kDa . The enzyme catalyzes the transfer of sialic acid to galactose-containing substrates, which is a crucial step in the biosynthesis of glycoproteins and glycolipids . This sialylation process is essential for various biological functions, including cell-cell interactions, immune responses, and pathogen recognition.
The enzyme shows a broad tissue distribution, with particularly high expression in the liver, lactating mammary gland, hematopoietic activated B cells, and subsets of T cells . Deficiency in ST6GAL1 results in a lack of α2,6-sialylation in N-linked glycans, which can lead to various biological consequences . The enzyme’s activity is also implicated in the generation of cell-surface carbohydrate determinants and differentiation antigens such as HB-6, CD75, and CD76 .
Recombinant ST6GAL1 expressed in sf9 cells is used in various research applications, including the study of glycosylation processes, the development of therapeutic glycoproteins, and the investigation of disease mechanisms related to sialylation . The enzyme’s role in immune responses and pathogen recognition makes it a valuable tool for studying infectious diseases and developing vaccines.
