The R-Spondin (Rspo) proteins belong to the Rspo family of Wnt modulators. Currently, the family consists of four structurally related secreted ligands (Rspo 1-4), all containing furin-like and thrombospondin structural domains. The Rspo proteins can interact with the Frizzled/LRP6 receptor complex in a manner that causes the stabilization and resulting accumulation of the intracellular signaling protein, ß-catenin. This activity effectively activates and increases the subsequent nuclear signaling of ß-catenin. R-Spondin can also bind to the previously discovered G-protein coupled receptors, LGR-4 and LGR-5. Rspo/ß-catenin signaling can act as an inducer of the transformed phenotype, and can also regulate the proliferation and differentiation of certain stem cell populations. Recombinant human R-Spondin-3 is a 26.9 kDa protein consisting of 240 amino acid residues. Due to glycosylation, R-Spondin-3 migrates at an apparent molecular weight of approximately 37.0 kDa by SDS PAGE analysis under reducing conditions.
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