Anti-ST6GALNAC4 antibody

Supplementary info

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

Activity summary

ST6GALNAC4 also known as ST6 N-acetylgalactosaminide alpha-26-sialyltransferase 4 is an enzyme involved in the biochemical process of transferring sialic acid to specific glycoproteins and glycolipids. This protein has a molecular mass of around 59 kDa. It operates within the Golgi apparatus where it contributes to the modification of glycoconjugates. Expression of ST6GALNAC4 occurs in various tissues but it shows higher activity in the brain and liver which suggests its importance in the function of these organs.

Biological function summary

ST6GALNAC4 serves in the synthesis and modification of sialylated glycoproteins. It plays an integral role in producing sialyl-Tn (sTn) antigen a sialylated glycan structure. The enzyme does not function as part of a large protein complex but interacts with other glycosyltransferases to achieve specific glycan modifications. These interactions are important for cellular communication adhesion and immune responses.

Pathways

ST6GALNAC4 is essential in the sialylation pathway influencing glycosylation patterns that affect cell surface properties. Glycosylation changes can modulate interactions with other proteins such as selectins and integrins. ST6GALNAC4 activity has implications for pathways related to cellular movement and interaction partially through the modulation of proteins like MUC1 a mucin involved in forming protective mucous barriers and signaling.

Associated diseases and disorders

ST6GALNAC4 connections appear significant in certain cancers and inflammatory conditions. The overexpression of sTn antigen resulting from ST6GALNAC4 activity is often linked to breast cancer aiding tumor progression and metastasis. Additionally aberrant sialylation by ST6GALNAC4 can affect immune response associating it with inflammatory bowel diseases. The protein's involvement with other enzymes such as ST6GAL1 helps modulate these disease pathways accentuating the role of glycosylation in disease development.