Recombinant Human Pofut1 protein (denatured)
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Recombinant Human Pofut1 protein (denatured) is a Human Full Length protein, in the 27 to 388 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE.
View Alternative Names
FUT12, KIAA0180, POFUT1, GDP-fucose protein O-fucosyltransferase 1, Peptide-O-fucosyltransferase 1, O-FucT-1
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human Pofut1 protein (denatured) (AB139789)
15% SDS-PAGE analysis of ab139789 (3μg).
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Pofut1 is responsible for the proper folding and functioning of specific proteins that undergo fucosylation. It does not technically form part of a multi-protein complex but interacts tightly with substrates it modifies. Through its enzymatic action Pofut1 influences essential biological activities in cell communication and signaling. This glycosyltransferase also plays a pivotal role in modulating Notch signaling a critical pathway in the development and tissue regeneration processes.
Pathways
The significance of Pofut1 is most notable within the Notch signaling pathway where it modifies the Notch receptor enabling effective ligand-receptor interactions. Dysregulation of this pathway can lead to critical developmental defects. Pofut1 also connects to other pathways such as the Fringe-mediated glycosylation pathway. In this context Pofut1-related proteins like Fringe glycosyltransferases operate to further influence Notch signaling outcomes through additional glycosylation processing.
Specifications
Form
Liquid
General info
Function
Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue found in the consensus sequence C2-X(4,5)-[S/T]-C3 of EGF domains, where C2 and C3 are the second and third conserved cysteines. Specifically uses GDP-fucose as donor substrate and proper disulfide pairing of the substrate EGF domains is required for fucose transfer. Plays a crucial role in NOTCH signaling. Initial fucosylation of NOTCH by POFUT1 generates a substrate for FRINGE/RFNG, an acetylglucosaminyltransferase that can then extend the fucosylation on the NOTCH EGF repeats. This extended fucosylation is required for optimal ligand binding and canonical NOTCH signaling induced by DLL1 or JAGGED1. Fucosylates AGRN and determines its ability to cluster acetylcholine receptors (AChRs).
Sequence similarities
Belongs to the glycosyltransferase 65 family.
Post-translational modifications
N-glycosylated.
Target data
Product promise
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