epitope corresponding to amino acids 21-300 mapping near the N-terminus of POFUT1 of human origin
Modification Notes
Glycosyltransferases that mediate the regio- and stereoselective transfer of sugars, such as the fucosyltransferases, determine cell surface-carbohydrate profiles, which is an essential interface for biological recognition processes. Fucosyltransferases catalyze the covalent association of fucose to different positional linkages in sugar acceptor molecules. POFUT1 (protein O-fucosyltransferase 1), also known as FUT12, O-FUT or O-FucT-1, is a 388 amino acid protein that localizes to the endoplasmic reticulum and belongs to the fucosyltransferase subfamily of glycosyltransferases. Highly expressed in pancreas, kidney, lung, heart, brain, liver, placenta and skeletal muscle, POFUT1 uses manganese to catalyze the attachment (specifically the O-glycosidic linkage) of fucose to a conserved serine or threonine residue on a protein acceptor. Via its cataytic activity, POFUT1 plays an important role in Notch signaling, as Notch ligands can serve as POFUT1 substrates. Two isoforms of POFUT1 exist due to alternative splicing events.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of POFUT1 of mouse, rat and human origin by WB, IP, IF and ELISA:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 21-300 mapping near the N-terminus of POFUT1 of human origin
Tissue Specificity
epitope corresponding to amino acids 21-300 mapping near the N-terminus of POFUT1 of human origin