Human FGF-9 Antibody
Human FGF-9 Antibody Summary
-7, -10, -11, -13, -16, -17, -18, -19, rhFGF acidic, rhFGF basic, recombinant mouse (rm) FGF‑6, -8b, -8c, or -15 is observed. In Western blots, no cross-reactivity with rhFGF-3, -4, -5, -6, -7, -10, -13, rmFGF-8b, or rmFGF-8c is observed.
Accession # P31371
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.
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.
The FGF family is comprised of at least nine polypeptides that show a variety of biological activities toward cells of mesenchymal, neuronal and epithelial origin. All FGFs have two conserved cysteine residues and share 30‑50% sequence identity at the amino acid level. FGF-9, also named glia-activating factor, was originally identified and purified from the supernatant of a human glioma cell line as a heparin-binding mitogenic growth factor for glial cells. FGF-9 has also been shown to stimulate the proliferation of oligodendrocyte type 2 astrocyte progenitor cells, Balb/c3T3 fibroblasts and PC-12 cells. However, unlike FGF acidic and basic, FGF-9 is not a mitogen for human umbilical vein endothelial cells.
The human FGF-9 cDNA encodes a 208 amino acid residue protein that contains a potential N-linked glycosylation site. The native protein is glycosylated. FGF-9 exhibits approximately 30% sequence similarity to other members of the FGF family. Although FGF-9 lacks a typical secretion signal, the protein is secreted efficiently after synthesis. Rat FGF-9 cDNA has been cloned and shown to be highly homologous to human FGF-9. The two proteins differ only in one amino acid residue. The expression of the FGF-9 transcripts has been shown to be restricted to the brain and the kidney.
- Naruo, K. et al. (1993) J. Biol. Chem. 268:2857.
- Miyamoto, M. et al. (1993) Mol. Cell Biol. 13:4251.
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