Detects human FGF-22 in direct ELISAs and Western blots. In Western blots, no cross-reactivity with recombinant human (rh) FGF-basic, rhFGF-3, -4, -5, -6, -7, -9, -10, -11, -12, -13, -16, -17, -18, -19, -20, -21, -23, recombinant mouse (rm) FGF-basic, rmFGF-8C, or -15 is observed.
Monoclonal Mouse IgG2A Clone # 435008
Protein A or G purified from hybridoma culture supernatant
E. coli-derived recombinant human FGF-22 Thr23-Ser170 Accession # Q9HCT0
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.
<0.10 EU per 1 μg of the antibody by the LAL method.
Measured by its ability to neutralize FGF‑22-induced proliferation in the 4MBr‑5 rhesus monkey epithelial cell line. The Neutralization Dose (ND50) is typically 1.5-7.5 µg/mL in the presence of 1 µg/mL Recombinant Human FGF‑22.
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.
Cell Proliferation Induced by FGF‑22 and Neutralization by Human FGF‑22 Antibody. Recombinant Human FGF‑22 (Catalog # 3867-FG) stimulates proliferation in the 4MBr‑5 rhesus monkey epithelial cell line in a dose‑dependent manner (orange line). Proliferation elicited by Recombinant Human FGF‑22 (1 µg/mL) is neutralized (green line) by increasing concentrations of Mouse Anti-Human FGF‑22 Monoclonal Antibody (Catalog # MAB3867). The ND50 is typically 1.5‑7.5 µg/mL.
Preparation and Storage
Reconstitute at 0.5 mg/mL in sterile PBS.
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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.
Fibroblast growth factor-22 (FGF-22) is a 23 kDa, non-glycosylated member of the FGF-7 subfamily, from the FGF family of heparin-binding growth factors (1‑3). The human FGF-22 precursor is 170 amino acids (aa) in length, and contains a 22 aa signal sequence with a 148 aa mature region (4‑6). The mature region shows a centrally-placed, 120 aa beta -trefoil region (aa 43‑168) that is characteristic of all FGF family members. Human FGF-22 potentially has one alternate splice form. This isoform is 129 aa in length, and shows a 31 aa substitution for the first N-terminal 72 aa of the standard, or long, form (7). There is no information related to its possible function. Mature human FGF-22 is 86% aa identical to mouse FGF-22, with the mouse molecule showing a 9 aa deletion at the N-terminus (5). FGF-22 is synthesized by at least three cell types; keratinocytes, neurons, and skeletal muscle myotubes (4, 8, 9). In neurons and myotubes, FGF-22 is presumed to function as an organizer of the presynaptic apparatus. Expressed by postsynaptic (or target) cells, FGF-22 is believed to bind to FGF R2b on the surface of innervating processes, resulting in synaptic vesicle clustering, organization, and neurite branching (8, 10). Although FGF-22 is assumed to be secreted, little can be found in expressing cell culture media. Presumably, it is bound to 34 kDa FGF-BP1, which is a molecule described as typically associated with cell membrane proteoglycans (6, 11). Thus, following secretion, FGF-22 could quickly be immobilized by FGF-BP1, only to be released at a later time, or aided by FGF-BP1 in its interaction with FGF R2b (6, 10, 11).
Itoh, N. and D.M. Ornitz (2004) Trends Genet. 20:563.
Ornitz, D.M. and N. Itoh (2001) Genome Biol. 2:3005.1 Epub 2001 Mar 9.
Nishimura, T. et al. (2000) Biochim. Biophys. Acta 1492:203.
Beyer, T.A. et al. (2003) Exp. Cell Res. 287:228.
Nakatake, Y. et al. (2001) Biochim. Biophys. Acta 1517:460.
Beer, H-D. et al. (2005) Oncogene 24:5269.
GenBank Accession # EAW61176.
Fox, M.A. and H. Umemori (2006) J. Neurochem. 97:1215.
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