LRP6 (C47E12) Rabbit mAb

LRP5 and LRP6 are single-pass transmembrane proteins belonging to the low-density lipoprotein receptor (LDLR)-related protein family. Unlike other members of the LDLR family, LRP5 and LRP6 have four EGF and three LDLR repeats in the extracellular domain, and proline-rich motifs in the cytoplasmic domain (1). They function as co-receptors for Wnt and are required for the canonical Wnt/β-catenin signaling pathway (2,3). LRP5 and LRP6 are highly homologous and have redundant roles during development (4,5). The activity of LRP5 and LRP6 can be inhibited by the binding of some members of the Dickkopf (DKK) family of proteins (6,7). Upon stimulation with Wnt, LRP6 is phosphorylated at multiple sites including Thr1479, Ser1490, and Thr1493 by kinases such as GSK-3 and CK1 (8-10). Phosphorylated LRP6 recruits axin to the membrane and presumably activates β-catenin signaling (8-10). 1.Brown, S.D. et al. (1998) Biochem. Biophys. Res. Commun. 248, 879-888. 2.Pinson, K.I. et al. (2000) Nature 407, 535-538. 3.Tamai, K. et al. (2000) Nature 407, 530-535. 4.Kelly, O.G. et al. (2004) Development 131, 2803-2815. 5.He, X. et al. (2004) Development 131, 1663-1677. 6.Semënov, M.V. et al. (2001) Curr Biol 11, 951-61. 7.Bafico, A. et al. (2001) Nat. Cell Biol. 3, 683-668. 8.Tamai, K. et al. (2004) Mol. Cell 13, 149-156. 9.Zeng, X. et al. (2005) Nature 438, 873-877. 10.Davidson, G. et al. (2005) Nature 438, 867-872.