FZD5 Extracellular Domain (human, recombinant)

Frizzled family G protein-coupled receptor 5 (FZD5) is a Wnt receptor involved in canonical and non-canonical Wnt/beta-catenin signaling. It is composed of an extracellular cysteine-rich ligand-binding domain, seven transmembrane domains, and an intracellular C-terminal domain that binds the PDZ domain of dishevelled (Dvl) and G proteins. Fzd5 is expressed in the yolk sac, eye, and lung during development and primarily in the eye, kidney, lung, and testis in adults. Upon ligand-binding, FZD5 associates with LDL receptor-related protein 5/6 (LRP5/6) and recruits Dvl, which leads to phosphorylation of LRP5/6, recruitment of Axin, and subsequent accumulation of beta-catenin. It is involved in ocular development, mesenchymal stem cell senescence, and intestinal crypt homeostasis, and plays pro- and anti-tumorigenic roles in a context-dependent manner. A frameshift mutation in FZD5 that results in production of a secreted FZD5 extracellular domain is associated with autosomal dominant coloboma. Cayman's FZD5 Extracellular Domain (human, recombinant) protein can be used for binding assays. This protein consists of 152 amino acids, has a calculated molecular weight of 17. kDa, and a predicted N-terminus of Ala27 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is 25-30 kDa due to glycosylation.