


Human Fibroblast Growth Factor 23 (R179Q)
SIZE
0.1 mg
INTRODUCTION
FGF-23 is a bone-derived hormone that acts in the kidney to regulate phosphate homeostasis and vitamin D metabolism. The signaling receptor for FGF-23, ɑ Klotho-FGFR1 (IIIc) complex, is an essential regulator of the renal sodium phosphate co-transporter and key vitamin D-metabolizing enzymes CYP27B1 and CYP24A1. Mature human FGF-23 contains an atypical (very low affinity) heparin binding site (aa 134-162), a proteolytic cleavage site (Arg179-Ser180), and multiple O-linked glycosylation sites with Thr178 being of particular importance. O-linked glycosylation at Thr178 blocks the cleavage of FGF-23, thereby preventing loss of FGF-23 activity. This recombinant human FGF23 bears mutation at 179th aa from arginine to glutamine preventing proteolytic cleavage.
DESCRIPTION
Expressed in E.coli with total 271 AA. Mw: 30.4 KDa (calculated).
N-terminal 6xHis-tag, EK and TEV cleavage site, 44 extra AA (highlighted).
Recombinant antigen for research use or manufacturing only.
SIZE
0.1 mg
INTRODUCTION
FGF-23 is a bone-derived hormone that acts in the kidney to regulate phosphate homeostasis and vitamin D metabolism. The signaling receptor for FGF-23, ɑ Klotho-FGFR1 (IIIc) complex, is an essential regulator of the renal sodium phosphate co-transporter and key vitamin D-metabolizing enzymes CYP27B1 and CYP24A1. Mature human FGF-23 contains an atypical (very low affinity) heparin binding site (aa 134-162), a proteolytic cleavage site (Arg179-Ser180), and multiple O-linked glycosylation sites with Thr178 being of particular importance. O-linked glycosylation at Thr178 blocks the cleavage of FGF-23, thereby preventing loss of FGF-23 activity. This recombinant human FGF23 bears mutation at 179th aa from arginine to glutamine preventing proteolytic cleavage.
DESCRIPTION
Expressed in E.coli with total 271 AA. Mw: 30.4 KDa (calculated).
N-terminal 6xHis-tag, EK and TEV cleavage site, 44 extra AA (highlighted).
Recombinant antigen for research use or manufacturing only.