Human POFUT1 protein (Recombinant) (N-GST & C-His) (STJP011000)

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STJP011000
€410.63 - €1,796.88
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Host: E. coli
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description : Recombinant-Human POFUT1-N-GST & C-His protein was developed from e. coli and has a target region of N-GST & C-His. For use in research applications.
Formulation: Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
Storage Instruction: Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at-20 to-80°C for twelve months from the date of receipt.
Gene Symbol: POFUT1
Gene ID: 23509
Uniprot ID: OFUT1_HUMAN
Immunogen Region: Leu284-Asp379
Immunogen: Homo sapiens (Human)
Post Translational Modifications N-glycosylated.
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).
Protein Name Gdp-Fucose Protein O-Fucosyltransferase 1
Peptide-O-Fucosyltransferase 1
O-Fuct-1
Database Links Reactome: R-HSA-1912399
Cellular Localisation Endoplasmic Reticulum
Alternative Protein Names Gdp-Fucose Protein O-Fucosyltransferase 1 protein
Peptide-O-Fucosyltransferase 1 protein
O-Fuct-1 protein
POFUT1 protein
FUT12 protein
KIAA0180 protein

Information sourced from Uniprot.org