Abcam, ab161069, Recombinant Human ST6GALNAC2 protein

Size: 10µg
Recombinant Human ST6GALNAC2 protein is a Human Full Length protein, in the 1 to 374 aa range, expressed in Wheat germ, suitable for ELISA, WB.
Key facts
Expression system:Wheat germ,
Tags:GST tag N-Terminus,
Applications:ELISA, WBSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:No,
Accession:Q9UJ37,
Animal free:No,
Carrier free:No,
Species:Human,
Storage buffer:pH: 8Constituents: 0.79% Tris HCl, 0.31% Glutathione

Properties and Storage Information:
Shipped at conditions-Dry Ice, Appropriate short-term storage conditions--80°C, Appropriate long-term storage conditions--80°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
ST6GALNAC2 also known as GalNAc α-26-sialyltransferase 2 is an enzyme involved in the sialylation process. Its molecular mass is approximately 56 kDa. The enzyme is expressed prominently in human tissues like the colon small intestine and spleen. ST6GALNAC2 catalyzes the transfer of sialic acid from CMP-NeuAc to GalNAc residues of glycoproteins and glycolipids playing a role in modifying their structures.
Biological function summary
The enzyme has a significant role in the biosynthesis of sialylated structures influencing cell-cell interactions signaling and immune modulation. ST6GALNAC2 is part of the glycosyltransferase family and it acts without forming larger complexes. Its activity affects the surface glycosylation pattern of cells influencing properties like cell adhesion and signaling pathways that are critical for cellular communication.
Pathways
Sialylation influences cellular interactions and immune responses and ST6GALNAC2's addition of sialic acid units impacts these processes. It participates in the glycosphingolipid biosynthesis pathway and influences the sialylation branch of the Nglycosylation pathway. ST6GALNAC2's activities interplay with other sialyltransferases in regulating the sialylation state of glycoproteins affecting interactions with receptors such as selectins and integrins which are important in mediating cellular adhesion and trafficking.
Altered ST6GALNAC2 activity links to colorectal cancer and inflammatory bowel diseases. In colorectal cancer modifications in glycosylation patterns influenced by ST6GALNAC2 and related enzymes like ST6GALNAC1 correlate with tumor progression and metastasis. In inflammatory bowel diseases the enzyme contributes to changes in the mucosal barrier affecting immune responses and tissue integrity. Understanding ST6GALNAC2's role offers insights into therapeutic targets in these diseases.