Leptin Receptor/CD295 Extracellular Domain (human, recombinant)

Leptin receptor, also known as CD295, is a leptin-binding transmembrane receptor with roles in the regulation of food intake, energy homeostasis, and lipid metabolism. It is composed of a multi-domain extracellular region comprising an N-terminal domain, a cytokine receptor homology (CRH1) domain, an immunoglobulin-like (Ig-like) domain, a CRH2 domain that binds leptin, and a fibronectin type III (FNIII) domain, a transmembrane domain, and an intracellular signaling domain. The leptin receptor is encoded by LEPR in humans and undergoes alternative splicing to form six isoforms, all of which are expressed in a tissue-dependent manner, contain identical extracellular regions, and have variable intracellular domains. Leptin receptor deficiency is induced by mutations in LEPR and is associated with hypothyroidism, hypogonadotropic hypogonadism, growth hormone deficiency, and extreme early-onset obesity. Cayman's Leptin Receptor/CD295 Extracellular Domain (human, recombinant) protein can be used for binding assay and Western blot (WB) applications. This protein consists of 829 amino acids, has a calculated molecular weight of 95 kDa, and a predicted N-terminus of Phe22 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is approximately 130-140 kDa due to glycosylation.