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Alternative Name : |
PRL-R, hPRLrI. |
Amount : |
20 µg |
Source : Escherichia Coli.
Extra Cellular Domain Prolactin Receptor Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containsing 210 amino acids and having a molecular mass of 23.97 kDa. The Prolactin Receptor is purified by proprietary chromatographic techniques according to Bignon et al. (1994) JBC 269; 3318-24 and tested according to Gertler et al. (1996) JBC 271; 24482-91.
Prolactin is a pituitary hormone that plays a role in the stimulation of milk production, salt and water regulation, growth, development and reproduction. The primary step in its action is the binding to a specific membrane receptor (prolactin receptor) which belongs to the superfamily of class 1 cytokine receptors. Prolactin is a hormone involved in a range of significant functions including ion transport and osmoregulation, stimulation of milk, protein synthesis as well as the regulation of numerous reproductive functions. Prolactin exerts its influence on different cell types through a signal transduction pathway which begins with the binding of the hormone to a transmembrane Prolactin receptor. PRLR varies in size (short and long forms) with tissue source and species, from ~40 kDa to 100 kDa. The PRL-R consists of at least 3 separate domains: an extracellular region with 5 cysteines which contains the prolactin binding site, a single transmembrane domain and a cytoplasmic region, the length of which appears to influence ligand binding and regulate cellular function.
It is recommended to reconstitute the lyophilized PRLR in sterile 18M-cm H2O not less than 100µg/ml and not more than 1 mg/ml, which can then be further diluted to other aqueous solutions. Activity is determined by the dose-dependant inhibition of Prolactin stimuled proliferation of Nb2 cells and by high affinity binding of ovine Prolactin and other lactogenic hormones in 1:1 molar ratio.