R-spondin-1 Fc fusion, human recombinant

$ 101.00

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  • RSPOFC-005 5 µg101.00
  • RSPOFC-025 25 µg301.00
  • RSPOFC-100 100 µg1001.00
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Source M.W. CAS No.
Structural Info
FormulationLyophilized in sterile filtered solution of PBS.
ReconstitutionBefore reconstitution, a brief spin is recommended to drive down any material dislodged from the bottom of the tube.  The lyophilized protein should be reconstituted in sterile H2O to a desired concentration.  
StabilityThe lyophilized protein is stable for at least one year if stored at -80 °C. Reconstituted protein is stable for at least four weeks at 4 °C, but should be stored in aliquots at -80 °C for longer term. Avoid repeated freeze and thaw.
PurityGreater than 90% as determined by SDS-PAGE analysis
Biological ActivityThe activity was determined by using a TCF reporter gene assay in cultured human cells. The EC50 ranges from 5 - 20 ng/ml in the presence of 10 ng/mL human WNT-3a.
Country of OriginUSA

R-spondin-1 is a natural enhancer of the canonical WNT pathway. When used together with WNT proteins that activate the
beta-catenin pathway, R-spondin-1 enhances the activity of canonical WNT proteins by binding to LGR5 and LGR4 (refs.)
Injection of recombinant R­Spondin-1 into mouse causes  activation of the β­catenin pathway and proliferation of intestinal crypt cells, which forms the basis for a clinical trial in amelioration of chemotherapy-induced colitis.

This product is the full-length R-Spondin-1 fused at its C-terminus to the Fc domain of human IgG1. This fusion increases the stability of the protein in vitro and in vivo without compromising its biological activity.  StemRD’s R-Spondin-1 Fc fusion protein is produced in human 293 cells as a secreted protein and purified by protein A chromatography.

Refs:  de Lau, et al, LGR5 homologues associate with Wnt receptors and mediate R-spondin signaling.  Nature. 2011 July 4; 476: 293;  
Carmon, et al, R-spondins function as ligands for the orphan receptors LGR4 and LGR5 to regulate Wnt/beta-catenin signaling. PNAS. 2011 Jul 12; 108: 11452.