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, beta-catenin. This activity effectively activates and increases the subsequent nuclear signaling of beta-catenin. R-Spondin can also bind to the previously discovered G-protein coupled receptors, LGR-4 and LGR-5. Rspo/beta-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-2 is a 24.4 kDa protein consisting of 212 amino acid residues. Due to glycosylation, R-Spondin-2 migrates at an apparent molecular weight of approximately 30.0 kDa by SDS PAGE analysis under reducing conditions.