Recombinant Human FGF-22 Protein

• Reactivity: Hu
• Applications: Bioactivity

Recombinant Human FGF-22 Protein Summary

• Details of Functionality: Measured in a cell proliferation assay using 4MBr‑5 rhesus monkey epithelial cells. Rubin, J.S. et al. (1989) Proc. Natl. Acad. Sci. USA 86:802. The ED₅₀ for this effect is 50-300 ng/mL.
• Source: E. coli-derived human FGF-22 protein
  Thr23-Ser170, with an N-terminal Met and 6-His tag
• Accession #: Q9HCT0
• N-terminal Sequence: Met
• Protein/Peptide Type: Recombinant Proteins
• Gene: FGF22
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain at 5 μg per lane
• Endotoxin Note: <0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Theoretical MW: 18 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.

Packaging, Storage & Formulations

• 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.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in MES, Na₂SO₄, EDTA, Sucrose and DTT with BSA as a carrier protein.
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain at 5 μg per lane
• Reconstitution Instructions: Reconstitute at 10 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human FGF-22 Protein

• FGF22
• FGF-22
• fibroblast growth factor 22

Background

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).

1. Itoh, N. and D.M. Ornitz (2004) Trends Genet. 20:563.
2. Ornitz, D.M. and N. Itoh (2001) Genome Biol. 2:3005.1 Epub 2001 Mar 9.
3. Nishimura, T. et al. (2000) Biochim. Biophys. Acta 1492:203.
4. Beyer, T.A. et al. (2003) Exp. Cell Res. 287:228.
5. Nakatake, Y. et al. (2001) Biochim. Biophys. Acta 1517:460.
6. Beer, H-D. et al. (2005) Oncogene 24:5269.
7. GenBank Accession #: EAW61176.
8. Fox, M.A. and H. Umemori (2006) J. Neurochem. 97:1215.
9. Umemori, H. et al. (2004) Cell 118:257.
10. Zhang, X. et al. (2006) J. Biol. Chem. 281:15694
11. Xie, B. et al. (2006) J. Biol. Chem. 281:1137.

Publications for FGF-22 (3867-FG)(4)

Publications using 3867-FG

• RO Costa, H Martins, LF Martins, AW Cwetsch, M Mele, JR Pedro, D Tomé, NL Jeon, L Cancedda, SR Jaffrey, RD Almeida Synaptogenesis Stimulates a Proteasome-Mediated Ribosome Reduction in Axons Cell Rep, 2019;28(4):864-876.e6. 2019 [PMID: 31340150] (Bioassay, Rat)
• Kanehira M, Kikuchi T, Santoso A, Tode N, Hirano T, Ohkouchi S, Tamada T, Sugiura H, Harigae H, Ichinose M Human marrow stromal cells downsize the stem cell fraction of lung cancers by fibroblast growth factor 10. Mol Cell Biol, 2014;34(15):2848-56. 2014 [PMID: 24865969] (Bioassay, Human)
• Wilson TR, Fridlyand J, Yan Y, Penuel E, Burton L, Chan E, Peng J, Lin E, Wang Y, Sosman J, Ribas A, Li J, Moffat J, Sutherlin DP, Koeppen H, Merchant M, Neve R, Settleman J Widespread potential for growth-factor-driven resistance to anticancer kinase inhibitors. Nature, 2012;487(7408):505-9. 2012 [PMID: 22763448] (Bioassay, Human)
• Tomlinson DC, Knowles MA Altered splicing of FGFR1 is associated with high tumor grade and stage and leads to increased sensitivity to FGF1 in bladder cancer. Am. J. Pathol., 2010;177(5):2379-86. 2010 [PMID: 20889570] (Bioassay, Human)

Bioinformatics

• Gene Symbol: FGF22
• Uniprot:
  • Q9HCT0()