Recombinant Mouse Prolactin Receptor (PRLR) Protein (His), Active

Name: Recombinant Mouse Prolactin Receptor (PRLR) Protein (His), Active
Brand: Beta LifeScience
SKU: BLC-05776P
Availability: InStock

Greater than 95% as determined by SDS-PAGE.

Activity Measured by its binding ability in a functional ELISA. Immobilized Mouse Prlr at 5 μg/ml can bind Anti-PRLR recombinant antibody , the EC 50 is 4.021-8.706 ng/mL.

Collections: Buy cytokines, chemokines, and growth factors for research online, Growth factors and receptors for advanced research, High-quality cytokines for advanced research, High-quality recombinant proteins, Recombinant proteins fall special offers - active proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Mouse Prolactin Receptor (PRLR) Protein (His), Active is produced by our Mammalian cell expression system. This is a protein fragment.
Purity	Greater than 95% as determined by SDS-PAGE.
Endotoxin	Less than 1.0 EU/ug as determined by LAL method.
Activity	Measured by its binding ability in a functional ELISA. Immobilized Mouse Prlr at 5 μg/mL can bind Anti-PRLR recombinant antibody , the EC 50 is 4.021-8.706 ng/mL.
Uniprotkb	Q08501
Target Symbol	PRLR
Synonyms	(PRL-R)
Species	Mus musculus (Mouse)
Expression System	Mammalian cell
Tag	C-10His
Target Protein Sequence	QSPPGKPEIHKCRSPDKETFTCWWNPGSDGGLPTNYSLTYSKEGEKNTYECPDYKTSGPNSCFFSKQYTSIWKIYIITVNATNEMGSSTSDPLYVDVTYIVEPEPPRNLTLEVKQLKDKKTYLWVKWLPPTITDVKTGWFTMEYEIRLKSEEADEWEIHFTGHQTQFKVFDLYPGQKYLVQTRCKPDHGYWSRWGQEKSIEIPNDFTLKD
Expression Range	20-229aa
Protein Length	Partial
Mol. Weight	27.3 kDa
Form	Lyophilized powder
Buffer	Lyophilized from a 0.2 μm filtered 20 mM Tris-HCl, 0.5 M NaCl, 6% Trehalose, pH 8.0
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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: 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

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.