Abcam, ab80076, Recombinant Human FUT5 protein

Size: 1mg
Recombinant Human FUT5 protein is a Human Fragment protein, in the 203 to 374 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, ELISA, WB.
Key facts
Purity:>90% SDS-PAGE,
Expression system:Escherichia coli,
Tags:Tag free,
Applications:ELISA, WB, SDS-PAGESee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:No,
Accession:Q11128,
Animal free:No,
Carrier free:No,
Species:Human,
Reconstitution:Reconstitute in 1 mL of water,
Storage buffer:Constituents: PBS

Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°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.
FUT5 also known as fucosyltransferase 5 is an enzyme with a mass of approximately 42 kDa. It is part of the fucosyltransferase family. FUT5 catalyzes the transfer of fucose from GDP-fucose to acceptor molecules such as glycoproteins and glycolipids. Mainly found in the Golgi apparatus FUT5 expression happens in tissues such as the colon liver and lungs. The enzyme plays a role in forming Lewis antigens important for cell-cell interactions.
Biological function summary
FUT5 contributes to the modification of glycoproteins and glycolipids impacting cellular adhesion and signaling mechanisms. This enzyme forms part of a biosynthetic complex involved in the creation of specific fucosylated structures. These structures participate in immune responses and development. FUT5 collaborates closely with other members of the fucosyltransferase enzyme family to determine glycan structures present on cell surfaces.
Pathways
FUT5 participates in the glycosphingolipid biosynthesis pathway and the protein glycosylation pathway. These pathways are important for cell communication and immune recognition. It collaborates with proteins like FUT3 and FUT6 sharing functional and structural similarities within these pathways. The glycosylation process involves multiple enzymes which ensure accurate structural formation of glycoproteins necessary for physiological processes.
FUT5 has been linked to certain types of cancer and inflammatory diseases. Aberrant expression or activity of FUT5 can influence cancer cell metastasis and tumor progression particularly in colorectal cancer. This enzyme is related to FUT3 known for its role in similar pathological conditions. Alterations in FUT5 activity might also contribute to inflammatory responses implicating it in immune system disorders.