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Recombinant human  Fibroblast growth factor receptor 1 (FGF-R1), protein kinase domain,10 µg  

Recombinant human Fibroblast growth factor receptor 1 (FGF-R1), protein kinase domain,10 µg

Recombinant human FGF-R1 (fibroblast growth factor receptor 1), tyrosine kinase domain, amino acids G400-R820, active enzyme

Alternate names: FGFR-1, BFGFR, CD331, CEK, FGFBR, FLG, FLT2, HBGFR, KAL2, N-SAM, FGF-R1 (fibroblast growth factor receptor 1) kinase, FGFR1

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Availability: on stock

295,00 €

Background: Fibroblast growth factor receptor (FGF-R) family consists of four genes encoding closely related transmembrane, tyrosine kinase receptors (termed FGF-R1 to FGF-R4). FGF bind in the presence of heparan sulfate proteoglucans (HSPG) to FGF-R forming a dimeric 2:2:2 FGF-FGFR-HSPG ternary complex on the cell surface. Complex formation induces receptor dimerization and a subsequent transphosphorylation of tyrosine residues in the activation loop of the kinase domain. Receptor activation regulates many key processes such as cell proliferation, survival, migration and differentiation by linking FGF-R to RAS / MAPK and PI3K / AKT and PKC pathways.

Protein: recombinant human FGF-R1 protein kinase domain (C-terminal fragment, amino acids G400-R820 ), N-terminally fused to GST-HIS6-Thrombin cleavage site

Theoretical MW : 78.1 kDa (fusion proteins)
Expression system: Sf9 cells
Purification: One-step affinity purification using glutathione agarose
Storage buffer: 50 mM Tris-HCl, pH 8.0; 100 mM NaCl, 5 mM DTT, 4 mM reduced glutathione, 20% glycerol
Protein concentration: 0.107 mg/ml (Bradford method using BSA as standard protein)
Method for determination of Km value & specific activity: Filter binding assay MAFC membrane
Specific activity : 22,000 pmol/mg  x min

Entrez Gene ID: 2260
UniProtKB: P11362

Ordering information: shipped on dry ice


Use the FGF-R1 - SPR Binding Assay of BIAFFIN for comprehensive kinetic characterization of your small molecule kinase inhibitors.



Figure: Real-time kinetic analysis of kinase inhibitor R-406 binding to FGF-R1 using surface plasmon resonance.

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Product specific literature:

Wesche J, Haglund K, Haugsten EM. (2011) "Fibroblast growth factors and their receptors in cancer." Biochem J. 437(2):199-213

Hu Y, Bouloux PM. (2010) "Novel insights in FGFR1 regulation: lessons from Kallmann syndrome." Trends Endocrinol Metab. 21(6):385-93.

Chen GJ, Forough R. (2006) "Fibroblast growth factors, fibroblast growth factor receptors, diseases, and drugs." Recent Pat Cardiovasc Drug Discov. (2):211-24.