Recombinant Mouse PRLR Protein (C-Fc)

Name: Recombinant Mouse PRLR Protein (C-Fc)
Brand: Beta LifeScience
SKU: BL-0142NP
Availability: InStock

BL-0142NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Mouse Prolactin Receptor is produced by our Mammalian expression system and the target gene encoding Gln20-Asp229 is expressed with a human IgG1 Fc tag at the C-terminus.
Accession	Q08501
Synonym	Prolactin receptor; PRL-R; Prlr; Prolactin R; PRLR
Gene Background	The prolactin receptor (PRLR) is a member of the class I cytokine/lactogen receptor family which mediates the diverse cellular actions of prolactin in several tissues. PRLRs are expressed in normal and neoplastic human breast tissue, and in most breast cancer cells. PRLR contains an extracellular region that binds prolactin, a transmembrane region, and a cytoplasmatic region required for the activation of the Jak2–Stat5 signal transduction pathway by Prl which is essential for transcriptional activation of all known prolactin regulated genes. PRLRs have also been observed in ovarian follicular cells of mice, pigs, sheep, deer, and humans, as well as in luteal tissue in cow and horse ovaries. Furthermore, PRLR knockout mice exhibit failure of embryonic implantation, reduced number of mature oocytes, and low fertilization rates. Knockout females also display a reduced number of primary follicles.
Molecular Mass	51.7 KDa
Apmol Mass	62-88 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	This is a receptor for the anterior pituitary hormone prolactin.
Subcellular Location	Membrane; Single-pass type I membrane protein.
Protein Families	Type I cytokine receptor family, Type 1 subfamily
Database References	KEGG: mmu:19116 STRING: 10090.ENSMUSP00000122219 UniGene: Mm.10516

Gene Functions References

Study shows prolactin receptors in Rip-cre cells, but not in AgRP neurones, are involved in energy homeostasis. Results indicate that Rip-Cre neurones in the arcuate nucleus are responsive to prolactin and may play a role in the orexigenic effects of prolactin, whereas prolactin does not directly affect Agrp neurones. PMID: 28378505
The estrogen-responsive pituitary hormone prolactin (PRL), through specific PRL receptor (PRLR), down-regulates hepatic triglyceride (TG) accumulation. PMID: 29524401
Truncating mutations of Prlr promote tumor growth in a model of human ERalpha+ breast cancer. PMID: 27681435
This study demonstrated that there are at least two functional subpopulations of dopamine neurons in the arcuate nucleus, with approximately 50% of these neurons expressing GABA. PMID: 27581458
Of the four placenta-specific, Prl-related hormones that have been shown to interact with the Prlr, their gene expression localizes to different endocrine cell types PMID: 26269505
Prolactin receptor was upregulated in proximal kidney tubule cells of mice with cardiac disease. PMID: 23712540
This study showed in knockout mice showed no effect of PRL and PRL-R gene ablation on heat and cold hyperalgesia in male mice, while heat hyperlgesia were reduced 3-72 h post-surgery in female PRL and PRL-R knockout mice PMID: 23994182
The in utero environment of the Prlr(+/-) mother confers long-term changes in the pancreatic islets of her offspring such that when the offspring themselves became pregnant, they cannot adapt to the increased insulin demands of their own pregnancy. PMID: 23247113
results provide direct genetic evidence that PRLR affects energy balance and metabolic adaptation in rodents via effects on brown adipose tissue differentiation and function PMID: 22637534
Germline knockout of prolactin or its receptor has failed to reveal a key role for prolactin signaling in mouse prostate physiology. PMID: 21971318
Data suggest that PRL stimulates the Prlr gene expression through the transcriptional activation of mE1(4) first exon, leading to increases in the long- and short-form variants of Prlr mRNA in the murine choroid plexus. PMID: 22294444
deactivation of MAPK by PRL/PRL-RS contributes to the severe ovarian defect in PRLR(-/-)RS mice and demonstrate the novel association of PRL-RS with DUPD1 and a role for this phosphatase in MAPK deactivation PMID: 21199871
Suggest that replacement of estrogen and progestin may not increase the mRNA of endometrial PRL receptor in metoclopromide-induced hyperprolactinemia in rats after castration. PMID: 19304288
Results provide a detailed mapping of the prolactin-responsive neurons in the female mouse forebrain by describing the distribution of prolactin receptor mRNA. PMID: 19882722
Pancreatic islets of PRLR-deficient mice were smaller, insulin mRNA levels were lower, glucose levels after an ip glucose load were higher PMID: 11897695
developmental defect of PrlR(-/-) mammary epithelium is rescued by an exogenously expressed chimeric receptor (prl-EpoR) containing the PrlR extracellular domain joined to the EpoR transmembrane and intracellular domains PMID: 12381781
results suggest that growth hormone can improve mammary development in prolactin receptor(+/-) mice, but that it fails to enhance metabolic activity PMID: 12399427
data suggest that CCAAT enhancer binding protein-beta is a master regulator of mammary epithelial cell fate and correct spatial pattern of progesterone receptor and prolactin receptor expression is critical for hormone-regulated cell proliferati PMID: 12456789
PR-1, the short form of the PRLR, can improve mammary development in PRLR+/- mice. This effect is probably caused by accelerated proliferation and an activation of the PRLR signaling cascade. PMID: 12624115
This protein and its substrates, expressed in murine hair follicle epithelium, show hair cycle-dependent expression, and induce catagen. PMID: 12707045
function of the SPRLR and a local and targeted effect of PRL on the mammary gland that are essential for its function, but not for its development. PMID: 12746331
results demonstrate that prostaglandin F2alpha inhibits the expression of the prolactin receptor PMID: 12865306
the absence of prolactin receptor signaling is not detrimental to male testicular function and to fertility in the mouse. PMID: 12933648
the expression of a constitutively active PRL-R by transgenesis induces a premature and abnormal mammary development and impairs terminal differentiation and milk production at the end of pregnancy. PMID: 14613905
These findings suggest a complex tissue-specific regulation of prolactin receptor expression in the context of the acute-phase response PMID: 15186999
different isoforms of prolactin receptors may be present in the various stages of mouse preimplantation embryo and may play an important role in the control of its growth and development PMID: 15820039
Cathepsin D secreted from various tissues is able to process PRL into 16K PRL outside the cell. PMID: 16959874
Report is the first in vivo demonstration that the action of pregnancy hormones, acting through Prlr, is required for normal maternal glucose tolerance during pregnancy by increasing beta-cell mass. PMID: 19036882
Prolactin independent rescue of mouse corpus luteum life span. PMID: 19531635

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.