Human FGF-18 Antibody Summary
Glu28-Ala207
Accession # O76093
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
Human FGF‑18 ELISA Standard Curve. Recombinant Human FGF‑18 protein was serially diluted 2-fold and captured by Mouse Anti-Human FGF‑18 Monoclonal Antibody (MAB667) coated on a Clear Polystyrene Microplate (Catalog # DY990). Mouse Anti-Human FGF‑18 Monoclonal Antibody (Catalog # MAB6672) was biotinylated and incubated with the protein captured on the plate. Detection of the standard curve was achieved by incubating Streptavidin-HRP (Catalog # DY998) followed by Substrate Solution (Catalog # DY999) and stopping the enzymatic reaction with Stop Solution (Catalog # DY994).
Reconstitution Calculator
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: FGF-18
Fibroblast Growth Factor 18 (FGF-18) is a 20 kDa protein that plays an important role in skeletal development and bone homeostasis (1). Mature human FGF-18 shares 99% amino acid sequence identity with mouse and rat FGF-18 (2). It is expressed in embryonic somites and the neural fold (3), adult lung (2), cerebellar and hippocampal neurons (4), hair follicle root sheath cells (5), and osteogenic mesenchymal cells (6). FGF-18 binds to FGF R2c, FGF R3c (4, 7) as well as the Golgi protein GLG1 (8) and induces the proliferation of astrocytes and microglia, vascular endothelial cells, dermal fibroblasts, papilla cells, and keratinocytes (4, 5, 9). FGF-18 is required for normal skeletal development (6). It recruits osteoclasts and osteoblasts to the growth plate, promotes osteoclast formation and function, inhibits osteoblast differentiation, promotes skeletal vascularization, and induces chondrocyte hypertrophy and cartilage matrix formation (6, 7, 10, 11).
- Beenken, A. and M. Mohammadi (2009) Nat. Rev. Drug Discov. 8:235.
- Ohbayashi, N. et al. (1998) J. Biol. Chem. 273:18161.
- Ohuchi, H. et al. (2000) Mech. Dev. 95:55.
- Hoshikawa, M. et al. (2002) Brain Res. Mol. Brain Res. 105:60.
- Kawano, M. et al. (2005) J. Invest. Dermatol. 124:877.
- Ohbayashi, N. et al. (2002) Genes Dev. 16:870.
- Davidson, D. et al. (2005) J. Biol. Chem. 280:20509.
- Miyaoka, Y. et al. (2010) Development 137:159.
- Hu, M.C. et al. (1998) Mol. Cell. Biol. 18:6063.
- Liu, Z. et al. (2007) Dev. Biol. 302:80.
- Shimoaka, T. et al. (2002) J. Biol. Chem. 277:7493.
Product Datasheets
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