Anti-Human FGF-23 Polyclonal Antibody (RMAB-0251571)
Cat. No.: RMAB-0251571
Category: Primary Antibodies
INQUIRY
50 μg
100 μg
Product Features
| Clonality | Polyclonal |
|---|---|
| Host Species | Rabbit |
| Immunogen | E.coli-derived, 25.5kDa Recombinant Human FGF-23 |
Target Information
| Target Symbol | FGF23 |
|---|---|
| Target Name | Fibroblast growth factor 23 |
| UniProt ID | Q9GZV9 |
| Cellular Localization | Secreted. Secretion is dependent on O-glycosylation. |
| Function | Regulator of phosphate homeostasis (PubMed:1162477). Inhibits renal tubular phosphate transport by reducing SLC34A1 levels (PubMed:114989). Up-regulates EGR1 expression in the presence of KL (By similarity). Acts directly on the parathyroid to decrease PTH secretion (By similarity). Regulator of vitamin-D metabolism (PubMed:154831). Negatively regulates osteoblast differentiation and matrix mineralization (PubMed:18282132). |
| Involvement in Disease | Hypophosphatemic rickets, autosomal dominant (ADHR): A disease characterized by isolated renal phosphate wasting, hypophosphatemia, and inappropriately normal 1,25-dihydroxyvitamin D3 (calcitriol) levels. Patients frequently present with bone pain, rickets, and tooth abscesses. The disease is caused by variants affecting the gene represented in this entry. Tumoral calcinosis, hyperphosphatemic, familial, 2 (HFTC2): A form of hyperphosphatemic tumoral calcinosis, a rare autosomal recessive metabolic disorder that manifests with hyperphosphatemia and massive calcium deposits in the skin and subcutaneous tissues. Some patients have recurrent, transient, painful swellings of the long bones associated with the radiographic findings of periosteal reaction and cortical hyperostosis and absence of skin involvement. The disease is caused by variants affecting the gene represented in this entry. |
| Post-translational Modifications | Following secretion this protein is inactivated by cleavage into a N-terminal fragment and a C-terminal fragment. The processing is effected by proprotein convertases. O-glycosylated at Thr-171 and Thr-178 by GALNT3 and glycosylation of Thr-178 requires previous glycosylation at Thr171. Glycosylation is necessary for secretion; it blocks processing by proprotein convertases when the O-glycan is alpha 2,6-sialylated. Competition between proprotein convertase cleavage and block of cleavage by O-glycosylation determines the level of secreted active FGF23. Phosphorylation at Ser-18 mediated by FAM2C slows down glycosylation at Thr-178 notably. |
| Sequence Similarities | Belongs to the heparin-binding growth factors family. |
For research use only. Not for clinical use.
