Human CellExp LEPR/CD295, human recombinant protein
LEPR, CD295, DKFZp686B1731, LEP-R, OB-R, OBR, Leptin receptor
|Calculated MW||This protein is fused with Fc fragment of human IgG1 at the C-terminus and has a calculated MW of 121 kDa expressed. The predicted N-terminus is Phe22. Protein migrates as 150-165 kDa in reduced SDS-PAGE resulting from glycosylation.|
|Other Names||LEPR, CD295, DKFZp686B1731, LEP-R, OB-R, OBR, Leptin receptor|
|Results||Measured by its ability to inhibit Leptin-dependent proliferation of BaF3 mouse pro-B cells transfected with rhLEPR-Fc. The ED50 for this effect is typically 0.015-0.13 µg/ml in the presence of 3 ng/ml rhLeptin.|
|Application Notes||Centrifuge the vial prior to opening. Reconstitute in sterile PBS, pH 7.4 to a concentration of 50 µg/ml. Do not vortex. This solution can be stored at 2-8°C for up to 1 month. For extended storage, it is recommended to store at -20°C.|
|Storage||-20°C; Lyophilized from 0.22 µm filtered solution in PBS, pH 7.4. Normally Mannitol or Trehalose is added as protectants before lyophilization.|
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Provided below are standard protocols that you may find useful for product applications.
Leptin receptor (LEPR), also known as LEP-R, cluster of differentiation 295 (CD295), OB-R and B219, is a single-transmembrane-domain receptor of the gp130 family of cytokine receptors. Leptin receptor exists as homodimer and binds Leptin with high affinity, thus mediates the biological function of the adipocyte-specific hormone Leptin. LEPR is a receptor for leptin (an adipocyte-specific hormone that regulates body weight), and is involved in the regulation of fat metabolism, as well as in a novel hematopoietic pathway that is required for normal lymphopoiesis. Mutations in this protein have been associated with obesity and pituitary dysfunction. Interaction of leptin and leptin receptor is crucial for body weight and bone mass regulation in mammals through hypothalamic effects on satiety and energy expenditure. Meanwhile, research data supports a leptin receptor activation model based on ligand-induced conformational changes.
Tartaglia L.A.,et al.Cell 83:1263-1271(1995).
Bennett B.D.,et al.Curr. Biol. 6:1170-1180(1996).
Cioffi J.A.,et al.Nat. Med. 2:585-589(1996).
Thompson D.B.,et al.Hum. Mol. Genet. 6:675-679(1997).
Luoh S.-M.,et al.J. Mol. Endocrinol. 18:77-85(1997).
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