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, β-catenin. This activity effectively activates and increases the subsequent nuclear signaling of β-catenin. R-Spondin can also bind to the previously discovered G-protein coupled receptors, LGR-4 and LGR-5. Rspo/β-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.
Roof plate-specific spondin-3, RSPO3, PWTSR, THSD2
MHPNVSQGCQ GGCATCSDYN GCLSCKPRLF FALERIGMKQ IGVCLSSCPS GYYGTRYPDI NKCTKCKADC DTCFNKNFCT KCKSGFYLHL GKCLDNCPEG LEANNHTMEC VSIVHCEVSE WNPWSPCTKK GKTCGFKRGT ETRVREIIQH PSAKGNLCPP TNETRKCTVQ RKKCQKGERG KKGRERKRKK PNKGESKEAI PDSKSLESSK EIPEQRENKQ QQKKRKVQDK QKSVSVSTVH
≥ 95% by SDS-PAGE gel and HPLC analyses.
R-Spondin-3 enhances BMP-2-mediated differentiation of MC3T3-E1 cells. The expected ED50 for this effect is 0.8 – 2.0 μg/ml.
Calculated Molecular Weight: