Anti-LRP6, clone Heldy-1-4 (rec.)

Wnt/beta-catenin signaling acts as a regulator of tissue development and homeostasis. Wnt ligands bind to a member of the Frizzled family of seven-transmembrane proteins and to either highly homologous low-density lipoprotein related receptors 5 (LRP5) or LRP6. Low-density lipoprotein receptor-related protein 6 (LRP6) is a member of the low-density lipoprotein receptor (LDLR) family. LRP5 and LRP6 are expressed in most human tissues and is composed of three distinctive cell-surface protein domains, including (1) LDL receptor (LDLR) type A repeats, (2) an epidermal growth factor (EGF)-like domain, and (3) a YWTD (Tyr-Trp-Thr-Asp)-type beta propeller domain. LRP6 is inhibited by the Dickkopf protein Dkk1 bound to their partners Kremen. Sclerotin also acts as an inhibitor of LRP5/6 through LRP4. LRP6 is involved in cell differentiation, proliferation and migration during embryonic development and in the pathogenesis of different cancer types. LRP6 plays a major role in metabolic regulation, specifically in the nutrient-sensing pathway. Patients carrying an LRP6 mutation exhibit high serum LDL cholesterol and triglycerides, hypertension, high fasting blood glucose levels, a prevalence of diabetes and low bone density. LRP6 mutations have also been associated with diseases such as Alzheimer's and degenerative joint diseases. LRP5, low-density-lipoprotein-receptor-related protein 5, is a determinant for bone mineral density and plays a role in osteoporosis. LRP5 is aso involved in vitreoretinopathy. Protein function: Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers beta-catenin signaling through inducing aggregation of receptor- ligand complexes into ribosome-sized signalsomes. Cell-surface coreceptor of Wnt/beta-catenin signaling, which plays a pivotal role in bone formation. The Wnt-induced Fzd/LRP6 coreceptor complex recruits DVL1 polymers to the plasma membrane which, in turn, recruits the AXIN1/GSK3B-complex to the cell surface promoting the formation of signalsomes and inhibiting AXIN1/GSK3- mediated phosphorylation and destruction of beta-catenin. Required for posterior patterning of the epiblast during gastrulation. [The UniProt Consortium]