Recombinant Human ST6GAL1 protein (His tag)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

ST6GAL1 is an enzyme that belongs to the glycosyltransferase family specifically classified as a sialyltransferase. ST6GAL1 catalyzes the addition of sialic acid to glycoproteins and glycolipids impacting their function and stability. It has an approximate molecular mass of 45 kDa. ST6GAL1 is expressed in a variety of cell types including B lymphocytes and epithelial cells. Its expression can be observed on the cell surface where it plays important roles in cell-cell interactions.

Biological function summary

ST6GAL1 contributes to the mechanics of cell signaling and immune system modulation. ST6GAL1 is involved in the biosynthesis of sialylated glycoconjugates which affect cellular recognition and communication. This enzyme does not form part of a multi-protein complex but interacts with other proteins upon glycosylation events. Through its action ST6GAL1 impacts multiple cellular processes including inflammation regulation and pathogen recognition.

Pathways

ST6GAL1 plays roles in glycosylation and immune response mechanisms. It participates in the N-glycan biosynthesis pathway which influences protein folding and stability. Additionally ST6GAL1 impacts the sialylation pathway where it modifies the surface proteins for lymphocyte activation. Importantly ST6GAL1 interacts with proteins such as Siglecs which are involved in immune response modulation and cellular recognition.

ST6GAL1 is implicated in cancer progression and autoimmune diseases. In various cancers such as colon cancer altered ST6GAL1 expression affects metastatic potential and tumor cell survival. Additionally aberrant ST6GAL1 expression occurs in autoimmune diseases like lupus wherein it modulates immune cell activity. ST6GAL1 interacts with proteins like CD22 a sialic acid-binding lectin on B cells influencing disease pathogenesis and progression through immune system pathways.