Recombinant Human FGF-BP Protein, CF Summary
Product Specifications
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.
Lys24-Cys234 & Asn29-Cys234 both with a C-terminal 10-His tag
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
1593-FB
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
Reconstitution | Reconstitute at 100 μg/mL in sterile PBS. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Reconstitution Calculator
Background: FGF-BP
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).
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- Tassi, E. et al. (2006) Cancer Res. 66:1191.
- Lametsch, R. et al. (2000) J. Biol. Chem. 275:19469.
- Xie, B. et al. (2006) J. Biol. Chem. 281:1137.
- Aigner, A. et al. (2002) Histochem. Cell Biol. 117:1.
- Beer, H.-D. et al. (2005) Oncogene 24:5269.
- Ray, P.E. et al. (2006) Am. J. Physiol. Regul. Integr. Comp. Physiol. 290:R105.
- Tassi, E. et al. (2007) Am. J. Physiol. Regul. Integr. Comp. Physiol. 293:R775.
- Kurtz, A. et al. (2004) Neoplasia 6:595.
- Tassi, E. et al. (2001) J. Biol. Chem. 276:40247.
- Mongiat, M. et al. (2001) J. Biol. Chem. 276:10263.
- Kurtz, A. et al. (1997) Oncogene 14:2671.
- Aigner, A. et al. (2001) Int. J. Cancer 92:510.
- Czubayko, F. et al. (1997) Nat. Med. 3:1137.
Citations for Recombinant Human FGF-BP Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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Widespread potential for growth-factor-driven resistance to anticancer kinase inhibitors.
Authors: 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
Nature, 2012-07-26;487(7408):505-9.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay -
Impact of fibroblast growth factor-binding protein-1 expression on angiogenesis and wound healing.
Authors: 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
Am. J. Pathol., 2011-09-21;179(5):2220-32.
Applications: Western Blot
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