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Mouse Anti-FGF23 Recombinant Antibody (FGF23/638) (CBMAB-F2324-CQ)

This product is a mouse antibody that recognizes FGF23. The antibody FGF23/638 can be used for immunoassay techniques such as: ELISA, FuncS.
See all FGF23 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
FGF23/638
Antibody Isotype
IgG1, κ
Application
ELISA, FuncS

Basic Information

Immunogen
A recombinant human FGF-23 protein
Specificity
Human
Antibody Isotype
IgG1, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS
Concentration
1 mg/mL
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Fibroblast Growth Factor 23
Introduction
This gene encodes a member of the fibroblast growth factor family of proteins, which possess broad mitogenic and cell survival activities and are involved in a variety of biological processes. The product of this gene regulates phosphate homeostasis and transport in the kidney. The full-length, functional protein may be deactivated via cleavage into N-terminal and C-terminal chains. Mutation of this cleavage site causes autosomal dominant hypophosphatemic rickets (ADHR). Mutations in this gene are also associated with hyperphosphatemic familial tumoral calcinosis (HFTC).
Entrez Gene ID
8074
UniProt ID
Q9GZV9
Alternative Names
Fibroblast Growth Factor 23; Phosphatonin; HYPF; Tumor-Derived Hypophosphatemia Inducing Factor; Tumor-Derived Hypophosphatemia-Inducing Factor; FGF-23;
Research Area
Regulator of phosphate homeostasis. Inhibits renal tubular phosphate transport by reducing SLC34A1 levels. Upregulates 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. Negatively regulates osteoblast differentiation and matrix mineralization.
Biological Process
Animal organ morphogenesis Source: GO_Central
Cell differentiation Source: GO_Central
Cellular phosphate ion homeostasis Source: Ensembl
Cellular response to interleukin-6 Source: Ensembl
Cellular response to leptin stimulus Source: Ensembl
Cellular response to parathyroid hormone stimulus Source: Ensembl
Cellular response to vitamin D Source: Ensembl
Fibroblast growth factor receptor signaling pathway Source: GO_Central
MAPK cascade Source: Ensembl
Negative regulation of bone mineralization Source: UniProtKB
Negative regulation of hormone secretion Source: UniProtKB
Negative regulation of osteoblast differentiation Source: UniProtKB
Phosphate-containing compound metabolic process Source: Ensembl
Phosphate ion homeostasis Source: UniProtKB
Positive regulation of cell population proliferation Source: GO_Central
Positive regulation of ERK1 and ERK2 cascade Source: Ensembl
Positive regulation of gene expression Source: GO_Central
Positive regulation of MAPKKK cascade by fibroblast growth factor receptor signaling pathway Source: Ensembl
Positive regulation of protein phosphorylation Source: GO_Central
Positive regulation of transcription, DNA-templated Source: Ensembl
Positive regulation of vitamin D 24-hydroxylase activity Source: UniProtKB
Regulation of cell migration Source: GO_Central
Regulation of phosphate transport Source: UniProtKB
Response to magnesium ion Source: Ensembl
Response to sodium phosphate Source: Ensembl
Vitamin D catabolic process Source: UniProtKB
Cellular Location
Secreted. Secretion is dependent on O-glycosylation.
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.
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.
PTM
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 by GALT3. 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.

Alber, J., & Föller, M. (2022). Lactic acid induces fibroblast growth factor 23 (FGF23) production in UMR106 osteoblast-like cells. Molecular and Cellular Biochemistry, 477(2), 363-370.

Ewendt, F., Feger, M., & Föller, M. (2021). Role of fibroblast growth factor 23 (FGF23) and αKlotho in cancer. Frontiers in Cell and Developmental Biology, 8, 601006.

Feger, M., Ewendt, F., Strotmann, J., Schäffler, H., Kempe-Teufel, D., Glosse, P., ... & Föller, M. (2021). Glucocorticoids dexamethasone and prednisolone suppress fibroblast growth factor 23 (FGF23). Journal of Molecular Medicine, 99(5), 699-711.

Ivey-Miranda, J. B., Stewart, B., Cox, Z. L., McCallum, W., Maulion, C., Gleason, O., ... & Testani, J. M. (2021). FGF-23 (fibroblast growth factor-23) and cardiorenal interactions. Circulation: Heart Failure, 14(11), e008385.

Mace, M. L., Olgaard, K., & Lewin, E. (2020). New aspects of the kidney in the regulation of fibroblast growth factor 23 (FGF23) and mineral homeostasis. International journal of molecular sciences, 21(22), 8810.

Hanudel, M. R., Eisenga, M. F., Rappaport, M., Chua, K., Qiao, B., Jung, G., ... & Ganz, T. (2019). Effects of erythropoietin on fibroblast growth factor 23 in mice and humans. Nephrology Dialysis Transplantation, 34(12), 2057-2065.

Bär, L., Stournaras, C., Lang, F., & Föller, M. (2019). Regulation of fibroblast growth factor 23 (FGF 23) in health and disease. FEBS letters, 593(15), 1879-1900.

Czaya, B., & Faul, C. (2019). The role of fibroblast growth factor 23 in inflammation and anemia. International journal of molecular sciences, 20(17), 4195.

Daryadel, A., Bettoni, C., Haider, T., Imenez Silva, P. H., Schnitzbauer, U., Pastor-Arroyo, E. M., ... & Wagner, C. A. (2018). Erythropoietin stimulates fibroblast growth factor 23 (FGF23) in mice and men. Pflügers Archiv-European Journal of Physiology, 470(10), 1569-1582.

Bär, L., Feger, M., Fajol, A., Klotz, L. O., Zeng, S., Lang, F., ... & Föller, M. (2018). Insulin suppresses the production of fibroblast growth factor 23 (FGF23). Proceedings of the National Academy of Sciences, 115(22), 5804-5809.

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For research use only. Not intended for any clinical use.

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We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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