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

Name: Recombinant Human Prolactin Receptor (PRLR) Protein (His), Active
Brand: Beta LifeScience
SKU: BLC-05773P
Availability: InStock

Greater than 95% as determined by SDS-PAGE.

Activity Measured by its binding ability in a functional ELISA. Immobilized Human PRLR at 2 μg/ml can bind Anti-PRLR recombinant antibody , the EC 50 is 126.8-171.9 ng/mL. Biological Activity Assay

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

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 Human 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 Human PRLR at 2 μg/mL can bind Anti-PRLR recombinant antibody , the EC 50 is 126.8-171.9 ng/mL.
Uniprotkb	P16471
Target Symbol	PRLR
Synonyms	PRLR; Prolactin receptor; PRL-R
Species	Homo sapiens (Human)
Expression System	Mammalian cell
Tag	C-10His
Target Protein Sequence	QLPPGKPEIFKCRSPNKETFTCWWRPGTDGGLPTNYSLTYHREGETLMHECPDYITGGPNSCHFGKQYTSMWRTYIMMVNATNQMGSSFSDELYVDVTYIVQPDPPLELAVEVKQPEDRKPYLWIKWSPPTLIDLKTGWFTLLYEIRLKPEKAAEWEIHFAGQQTEFKILSLHPGQKYLVQVRCKPDHGYWSAWSPATFIQIPSDFTMND
Expression Range	25-234aa
Protein Length	Partial
Mol. Weight	27.2 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 (PRL). Acts as a prosurvival factor for spermatozoa by inhibiting sperm capacitation through suppression of SRC kinase activation and stimulation of AKT. Isoform 4 is unable to transduce prolactin signaling. Isoform 6 is unable to transduce prolactin signaling.
Subcellular Location	Membrane; Single-pass type I membrane protein.; [Isoform 7]: Secreted.
Protein Families	Type I cytokine receptor family, Type 1 subfamily
Database References	HGNC: 9446 OMIM: 176761 KEGG: hsa:5618 STRING: 9606.ENSP00000371432 UniGene: PMID: 28980840 Low PRLR expression is associated with Triple Negative Breast Cancer. PMID: 27480353 These results illustrate promising antitumor activity against PRLR-positive breast cancer xenografts and support the evaluation of anti-PRLR antibody-drug conjugate as potential therapeutic agents in breast cancer. PMID: 28377489 Prl receptor is expressed at different levels in the majority of glioblastoma multiforme tumors. Prolactin stimulation resulted in increased STAT5 phosphorylation and increased cellular invasion. PMID: 27788487 PRLRI146L and PRLRI176V variants are not associated with breast cancer or multiple breast fibroadenomas risk. PMID: 27575941 This study identified 4 PRLR variations (p.Ile76Val, p.Ile146Leu, p.Glu108Lys and p.Glu554Gln) in 16 Sporadic Prolactinoma in Humans. PMID: 26641246 results highlight PRLR as an independent predictor of favorable prognosis in human breast cancer PMID: 26317306 Two markers for the PRL peptide gene and three markers for the prolactin receptor (PRLR) gene were genotyped. PMID: 26513615 The prolactin receptor is constitutively expressed on regulatory T and effector T cells in systemic lupus erythematosus patients, and this expression is higher than in healthy individuals. PMID: 26844452 There is a possible role for PRLR in the progression of cervical cancer. PMID: 24990775 Study shows that position 146 plays a central role in directing intrinsic properties of the PRLR, including extracellular domain folding, PRL-responsiveness, and ligand-independent activity of the receptor. PMID: 25524456 Data suggest that (1) cell membrane/lipid bilayer binding of PRLR and (2) tyrosine phosphorylation of PRLR intracellular domain are independent. PMID: 25846210 long PRLR plays an important role in breast cancer metastasis. PMID: 26095602 a residue quartet in the extracellular membrane proximal domain of the homodimeric cytokine receptor prolactin receptor is a key regulator of intracellular signaling discrimination PMID: 25784554 PRL induced transient signaling pathways in neurons and modulated ion channels. [review] PMID: 24758841 exposure to prolactin increases TNF-alpha release from CD14(+) monocytes of rheumatoid arthritis patients, which can be abolished by PRLR gene silencing or treating with MAPK inhibitor. PMID: 24997655 High MFAB expression is associated with testicular germ cell tumor and glioblastomas. PMID: 24391856 Negative/low expression is associated with poorly differentiated and larger breast tumors in Poland PMID: 24249584 Major changes in prolactin receptor conformation and dimerization affinity are triggered by single mutations in critical regions of D1. PMID: 24735798 PRL-R attenuation post-transcriptionally increased ZnT2 abundance and redistributed intracellular Zn pools into lysosomes and mitochondria. PMID: 24333596 Hypertrimethylation on H3K27 of the p53 gene promoter region due to elevated expression of DeltaS2 PRLR by alternative splicing of the pre-mRNA in its full-length form might serve as a new mechanism underlying prostate cancer PMID: 24032713 Data suggest that signal transduction via prolactin and prolactin receptor plays role in trophoblast cell migration and invasion; PRLR is expressed by extravillous cytotrophoblasts and first-trimester placental bed tissue. PMID: 23849393 PRL-induced transient signaling in sensory neurons is governed by PI3K or PKCepsilon, mediated via the PRLR-S isoform, and transient effects mediated by PRLR-S are inhibited by presence of PRLR-L in these cells. PMID: 24142695 SNPs of the PRLR gene 5' UTR and promoter region are associated with increased risk for gestational diabetes in a population of Chilean subjects. PMID: 23651351 Thus, the familial hyperprolactinemia appears to be due to a germline, loss-of-function mutation in PRLR, resulting in prolactin insensitivity. PMID: 24195502 Results demonstrate a novel function for hepatic PRLR in the regulation of insulin sensitivity and provide important insights concerning the nutritional regulation of PRLR expression. PMID: 23775766 Our data suggest that prolactin receptor presence meaningfully affects growth hormone receptor use in breast cancer cells. PMID: 23192981 The prolactin receptor transactivation domain is associated with steroid hormone receptor expression and malignant progression of breast cancer PMID: 23159947 Our results indicate no significant association of prolactin and PRLR polymorphisms with clozapine response, tardive dyskinesia diagnosis or its severity in patients with schizophrenia PMID: 21305610 can be activated by three sequence-diverse human hormones: prolactin, GH, and placental lactogen [review] PMID: 22577091 PRLr isoforms expression and PRLr subcellular localisation are altered in parathyroid tumours PMID: 22606260 The structure of the human prolactin receptor reveals a structural link between the WSXWS motif, hormone binding, and receptor dimerization and we propose it as a general mechanism for class 1 receptor activation. PMID: 22325776 PRL signaling through the long form prolactin receptor causes reduced fatty acid oxidation, increased lipid storage, glucose intolerance, and obesity. PMID: 21989556 data provide limited support for an association between common variations in PRLR and breast cancer risk PMID: 21470416 The association of the PRLr with HMGN2 enables Stat5a-responsive promoter binding, thus facilitating transcriptional activation and promoting anchorage-independent growth. PMID: 21816901 Our study suggests the prolactin receptor gene is a molecular target that may be important in the pathogenesis and progression of lobular neoplasia PMID: 20658264 Enhanced complex formation of ERalpha dimer with SP1 and C/EBPbeta by E2 has an essential role in the transcriptional activation of the hPRLR gene. PMID: 21670145 Data show that cells expressing higher long:short PRLR ratios had increased growth, survival and migration in response to PRL and suggest that PRLR antagonists may be therapeutically beneficial in ovarian cancer. PMID: 21775057 Endogenous GH receptor(GHR) and PRLR associate, possibly as a GHR-PRLR heterodimer, in human breast cancer cells and GH signaling in these cells is largely mediated by the PRLR in the context of both PRLR-PRLR homodimers and GHR-PRLR heterodimers. PMID: 21310852 The positive correlations in positivity rate between the PRL-R and ER/PR expressions are found only in CerbB-2 positive patients with breast cancer. PMID: 20335148 SIRPalpha modulates PRL receptor-associated signaling as a function of integrin occupancy by mediating integrin-PRL receptor cross-talk and contributing to breast cancer biology. PMID: 20826546 both Zn(2+) and human PRLr binding influence human PRL conformers in an interdependent fashion PMID: 21510945 Functional impact of manipulation on the relative orientation of human prolactin receptor domains. PMID: 21591677 Progesterone induces expression of the prolactin receptor gene through cooperative action of Sp1 and C/EBP transcription factors PMID: 21238538 Rabbit antibodies have high titer and could specifically recognize each isoform of PRLR in breast cancer cell lines and human breast carcinoma biopsies. PMID: 21144038 Prolactin receptor signaling contributes to the local inflammatory response within the atherosclerotic plaque and thus to atherogenesis. PMID: 21068074 Blockade of the PRLR represents a novel treatment for patients with advanced breast or prostate cancer with limited therapeutic options. PMID: 20846877 acetylation and deacetylation provide the rheostat-like regulation for the cytokine receptor PRLR in its cytoplasmic loop dimerization and subsequent STAT5 activation PMID: 20962278 This study allowed to visualize for the first time the loop L5 spanning PRLR2 residues Thr133-Phe140, revealing its central implication for the three intermolecular interfaces of the 1:2 complex between natural prolactin and two PRLR chains. PMID: 20875426 prolactin receptor expression is common in colorectal cancer PMID: 20453834

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.