Mouse PRLR / Prolactin receptor Protein (His Tag)

Produkt-Information von PRLR / Prolactin receptor Protein

QC Testing von PRLR / Prolactin receptor Protein

Purity	>95% as determined by SDS-PAGE	SDS-PAGE: PRLR protein
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Stability	Samples are stable for up to twelve months from date of receipt at -70℃
Predicted N terminal	Gln 20
Molecular Mass	The recombinant mouse PRLR comprises 221 amino acids and has a predicted molecular mass of 26 kDa. The apparent molecular mass of the protein is approximately 37 kDa in SDS-PAGE under reducing conditions due to glycosylation.
Formulation	Lyophilized from a 0.2μm filtered solution of PBS, pH7.4. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.

Usage Guide von PRLR / Prolactin receptor Protein

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Beschreibung von PRLR / Prolactin receptor Protein

Prolactin receptor (PRLR) is a single-pass transmembrane receptor belonging to the type Ⅰ cytokine receptor superfamily, and contains two fibronectin type-Ⅲ domains. PRLR is widely expressed in breast, placenta, kidney, liver and pancreas, and mainly serves as the receptor for the pituitary hormone prolactin (PRL) , a secreted hormone that affects reproduction and homeostasis in vertebrates. All class 1 ligands activate their respective receptors by clustering mechanisms. Ligand binding results in the transmembrane PRLR dimerization, followed by phosphorylation and activation of the molecules invloved in the signaling pathways, such as Jak-STAT, Ras/Raf/MAPK. It has been shown that specific binding to PRLR can stimulate the breast cancer cells to grow and certain antagonists which bind but do not dimerize PRLR can inhibit the growth of breast cancer cells. Several isoforms have been described, and the soluble form are unable to transduce prolactin signaling.

References

1. Somers W. et al., 1994, Nature. 372: 478-81.
2. Fuh G. et al., 1995, J Biol Chem. 270: 13133-7.
3. Kline JB. et al., 1999, J Biol Chem. 274: 35461-8.
4. Svensson LA. et al., 2008, J Biol Chem. 283: 19085-94.

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