Leptin R in Rat Brain. |
Leptin R was detected in perfusion fixed frozen sections of rat brain using 15 µg/mL Goat Anti-Mouse Leptin R Antigen Affinity-purified Polyclonal Antibody (Catalog # AF497) overnight at 4 °C. Tissue was stained with the Anti-Goat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS008) and counterstained with hematoxylin (blue). Specific labeling was localized to the cytoplasm of cells in the choroid plexus. View our protocol for Chromogenic IHC Staining of Frozen Tissue Sections.
Leptin receptor (OB-R), also named B219, is a type I cytokine receptor family protein with significant amino acid sequence identity with gp130, G-CSF receptor, and the LIF receptor. Multiple isoforms of human and mouse OB-R, including a long form (OB-RL) with a large cytoplasmic domain capable of signal-transduction, and several receptor isoforms with short cytoplasmic domains (OB-Rs) lacking signal-transducing capabilities, have been identified. The extracellular domains of the short and long forms of OB-R are identical. An OB-R transcript lacking a transmembrane domain and potentially encoding a soluble form of the receptor has also been described. Circulating soluble OB-R, complexed to leptin, has been detected in mouse serum. Serum soluble OB-R levels have been shown to increase during pregnancy. OB-RL transcripts were reported to be expressed predominantly in regions of the hypothalamus previously thought to be important in body weight regulation. Expression of OB-Rs transcripts have been found in multiple tissues, including the choroid plexus, lung, kidney and primitive hematopoietic cell populations. OB-R has recently been shown to be encoded by the mouse diabetes (db) and rat fatty (fa) genes. Rodents homozygous for the db or fa mutations have been known to exhibit an obesity phenotype.
Mouse OB-R long form encodes a 1162 amino acid (aa) residue precursor protein with a 22 aa residue signal peptide, an 817 aa residue extracellular domain, a 21 aa residue transmembrane domain, and a 302 aa residue cytoplasmic domain. The extracellular domain of OB-R contains two hemopoietin receptor domains, a fibronectin type III domain and the WSXWS domain. Recombinant murine soluble OB-R has been shown to bind leptin with high affinity and is a potent leptin antagonist.
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