Recombinant Human FGF-BP Protein, CF

• Reactivity: Hu
• Applications: Binding Activity
• Format: Carrier-Free

Recombinant Human FGF-BP Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. 1 μg/mL of rhFGF-BP was mixed with serially diluted rhFGF basic (Catalog # 233-FB). Following incubation, the FGFBP-FGF basic complex was captured on a Gt x hFGFBP-coated plate. Bound FGF basic was measured using biotinylated Gt x hFGF basic. The concentration of rhFGF basic that produces 50% of the optimal binding was found to be approximately 5-20 ng/mL.
• Source: Mouse myeloma cell line, NS0-derived human FGF-BP protein Lys24-Cys234 & Asn29-Cys234 both with a C-terminal 10-His tag
• Accession #: Q14512
• N-terminal Sequence: Lys24 & Asn29
• Protein/Peptide Type: Recombinant Proteins
• Gene: FGFBP1
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Endotoxin Note: <1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Binding Activity
• Theoretical MW: 25.2 kDa & 24.6 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.
• SDS-PAGE: 31-35 kDa, reducing conditions

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  12 months from date of receipt, -20 to -70 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 3 months, -20 to -70 degreesC under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS.
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Reconstitution Instructions: Reconstitute at 100 μg/mL in sterile PBS.

Notes

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

Alternate Names for Recombinant Human FGF-BP Protein, CF

• 17 kDa heparin-binding growth factor-binding protein
• FGFBP
• FGF-BP
• FGFBP1
• FGF-BP1
• FGFBP-1
• FGFBPFGF-binding protein 1
• fibroblast growth factor binding protein 1
• fibroblast growth factor-binding protein 1
• HBp17
• HBP1717 kDa HBGF-binding protein
• heparin-binding growth factor binding protein

Background

Fibroblast growth factor binding protein (FGF-BP), also known as HBp17, is a secreted glycoprotein that increases the bioavailability of FGFs (1). Mature FGF-BP is a 34 kDa, 211 amino acid (aa) O-glycosylated protein with five conserved intrachain disulfide bonds (2 - 4). FGF-BP contains a heparin-binding domain (aa 110 - 143) and a distinct FGF-binding region (aa 193 - 243) (5). Mature human FGF-BP shares 59% and 54% aa sequence identity with mouse and rat FGF-BP, respectively. FGF-BP is expressed throughout development and in adult squamous epithelium (2, 6). It is upregulated in injured skin, renal tubular epithelium, and spinal nerves as well as in carcinomas of the skin, colon, and pancreas (3, 7 - 10). FGF-BP binds FGF-1, -2, -7, -10, and -22 which are secreted and sequestered in the extracellular matrix (ECM) (7, 11). The association of FGF-BP with heparan sulfate proteoglycans (HSPG) weakens HSPG attachment of FGFs and promotes their release (2, 8, 12, 13). FGF-BP enhances the mitogenic effects of FGFs, thereby contributing to epithelial, endothelial, and neuronal tissue repair, angiogenesis, and tumor growth (7 - 9, 11, 14, 15).

1. Abuharbeid, S. et al. (2006) Int. J. Biochem. Cell Biol. 38:1463.
2. Wu, D. et al. (1991) J. Biol. Chem. 266:16778.
3. Tassi, E. et al. (2006) Cancer Res. 66:1191.
4. Lametsch, R. et al. (2000) J. Biol. Chem. 275:19469.
5. Xie, B. et al. (2006) J. Biol. Chem. 281:1137.
6. Aigner, A. et al. (2002) Histochem. Cell Biol. 117:1.
7. Beer, H.-D. et al. (2005) Oncogene 24:5269.
8. Ray, P.E. et al. (2006) Am. J. Physiol. Regul. Integr. Comp. Physiol. 290:R105.
9. Tassi, E. et al. (2007) Am. J. Physiol. Regul. Integr. Comp. Physiol. 293:R775.
10. Kurtz, A. et al. (2004) Neoplasia 6:595.
11. Tassi, E. et al. (2001) J. Biol. Chem. 276:40247.
12. Mongiat, M. et al. (2001) J. Biol. Chem. 276:10263.
13. Kurtz, A. et al. (1997) Oncogene 14:2671.
14. Aigner, A. et al. (2001) Int. J. Cancer 92:510.
15. Czubayko, F. et al. (1997) Nat. Med. 3:1137.

Publications for FGF-BP (1593-FB)(2)

Publications using 1593-FB

• 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, 2012-07-26;487(7408):505-9. 2012-07-26 [PMID: 22763448] (Bioassay, Human)
• Tassi E, McDonnell K, Gibby KA, Tilan JU, Kim SE, Kodack DP, Schmidt MO, Sharif GM, Wilcox CS, Welch WJ, Gallicano GI, Johnson MD, Riegel AT, Wellstein A Impact of fibroblast growth factor-binding protein-1 expression on angiogenesis and wound healing. Am. J. Pathol., 2011-09-21;179(5):2220-32. 2011-09-21 [PMID: 21945411] (Western Blot)

Bioinformatics

• Gene Symbol: FGFBP1
• Uniprot:
  • Q14512()