金山科研平台，产品价格货期咨询微信：jinshanbio Source:Chinese Hamster Ovary cell line, CHO-derived, Met1-Gly205 Accession #:NP_766403 N-terminal Sequence Analysis:Predicted Gln22, not observed that sequencing might be blocked & Ala32 Purity:>95%, by SDS-PAGE under reducing conditions and visualized by silver stain. Predicted Molecular Mass:21 kDa &20 kDa SDS-PAGE:26-27 kDa, reducing conditions Activity:Measured by its ability to induce activation of beta -catenin response in a Super (16X) Topflash Luciferase assay using HEK293T human embryonic kidney cells.The ED₅₀ for this effect is typically 3 - 15 ng/mL in the presence of 5 ng/mL Recombinant Mouse Wnt-3a (Catalog# 1324-WN). Molecule Information: R-Spondin 2 Long Name: Roof Plate-specific Spondin 2 Aliases: Cristin 2; RSPO2 Entrez Gene IDs: 340419 (Human); 239405 (Mouse) Background: R-Spondin 2 R-Spondin 2 (RSPO2, Roof plate-specific Spondin 2), also known as cysteine-rich and single thrombospondin domain containing protein 2 (Cristin2), is a 33kDa secreted protein that belongs to the R-Spondin family. The four known human R-Spondins regulate ß-catenin signaling and overlap in expression and function. Like other R-Spondins, R-Spondin 2 contains two adjacent cysteine-rich furin-like domains (aa90-134) followed by a thrombospondin (TSP-1) motif (aa144-204) and a C-terminal region rich in basic residues (aa 207-243). The basic region appears to mediate cell surface retention but not to influence function (1). R-Spondin2 contains one potential N-glycosylation site. Of the three reported splice isoforms of human R-Spondin 2, isoform2 lacks residues1-67 of isoform1, while isoform3 has a glycine substitution for residues 32-95 of isoform1. Human R-Spondin 2 is expressed in organs of endodermal origin in adults, including intestine and lung, and is downregulated in tumors of these tissues. In the embryonic mouse, R-Spondin 2 is expressed most highly in the hippocampus and in developing teeth and bones. Studies in Xenopus and mouse embryos indicate that R-Spondin 2 is an extracellular activator of Wnt/ß-catenin signaling and is required for myogenesis. Mouse R-Spondinproteins bind both LRP-6 and Frizzled-8 but do not appear to form a ternary complex (3). R-Spondin 2 over-expression in Xenopus also blocks signaling of TGF-beta ligands, activin, nodal and BMP-4 (1). Human R-Spondin 2 is highly conserved across species, sharing 97-98%aa identity with mouse, rat, canine,bovine, and opossum R-Spondin 2 and 86% aa identity with Xenopus R-Spondin2 within aa22-205. Mature R-Spondin 2 shares ~40% aa identity with R-Spondin 1, R-Spondin 3, and R-Spondin 4.