Recombinant Rat Prolactin Protein (PRL), Active

Name: Recombinant Rat Prolactin Protein (PRL), Active
Brand: Beta LifeScience
SKU: BLC-05554P
Availability: InStock

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Product Overview

Description	Recombinant Rat Prolactin Protein (PRL), Active is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 98% as determined by SDS-PAGE and HPLC.
Endotoxin	Less than 1.0 EU/μg as determined by LAL method.
Activity	Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using rat Nb2-11 cells is less than 1.0 ng/ml, corresponding to a specific activity of >1.0x10 6 IU/mg.
Uniprotkb	P01237
Target Symbol	PRL
Synonyms	Prl; Prolactin; PRL
Species	Rattus norvegicus (Rat)
Expression System	E.Coli
Tag	Tag-Free
Complete Sequence	LPVCSGGDCQ TPLPELFDRV VMLSHYIHTL YTDMFIEFDK QYVQDREFIA KAINDCPTSS LATPEDKEQA QKVPPEVLLN LILSLVHSWN DPLFQLITGL GGIHEAPDAI ISRAKEIEEQ NKRLLEGIEK IISQAYPEAK GNEIYLVWSQ LPSLQGVDEE SKDLAFYNNI RCLRRDSHKV DNYLKFLRCQ IVHKNNC
Expression Range	30-226aa
Protein Length	Full Length of Mature Protein
Mol. Weight	22.6 kDa
Research Area	Signal Transduction
Form	Lyophilized powder
Buffer	Lyophilized from a 0.2 µm filtered PBS, pH 7.4
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	Prolactin acts primarily on the mammary gland by promoting lactation.
Subcellular Location	Secreted.
Protein Families	Somatotropin/prolactin family
Database References	KEGG: rno:24683 STRING: 10116.ENSRNOP00000023412 UniGene: PMID: 28988314 Data suggest that prolactin and oleic acid synergistically stimulate beta-cell proliferation and islet growth; in cultured neonatal islets, prolactin increases cell proliferation 6-fold, oleic acid 3.5-fold, and their combination 15-fold. Similar results were observed in cultured adult islets. PMID: 28686504 Involvement of prolactin in the regulation of bicarbonate biodynamics using female rat model of cholestasis of pregnancy. PMID: 28361424 This study reports on the effect of copulation on potentially precancerous prostate lesions, serum testosterone and prolactin levels in rats. PMID: 27356573 This study demonstrated that the Cultured neurons expressed mRNA for both PRL and its receptor (PRLR), and both PRL and PRLR expression levels changed after the excitotoxic insult. PMID: 26874070 Data confirm that prolactin secretion by anterior pituitary gland can be down-regulated by environmental endocrine disruptors; here, perfluorooctane sulfonate affects periventricular-hypophysial dopaminergic neurons in mechanism involving estradiol. PMID: 26032630 In conclusion, PRL was responsible for the lactation-induced mucosal adaptations, which were associated with compensatory increase in FGF-23 expression probably to prevent calcium hyperabsorption. PMID: 26657069 PRL is unchanged in a rat model of panic evoked by dorsal periaqueductal gray stimulation. PMID: 25618592 Prolactin actively supports lactation providing amino acids to the gland through SNAT2 for the synthesis of milk proteins. PMID: 25701231 Results showed that an active sexual life, with constant execution of sexual behavior, produces a sustained increase in serum PRL, prostate PRL receptors, and the pStat3 signaling pathway PMID: 25446202 This study showe that TGF-beta and TNF-alpha antagonize the effect of each other on the expression and release of prolactin in a cell line and in obese and diabetic rats. PMID: 25715833 supraphysiological levels of PRL affect carcinogenesis. PL induces regression of the tumors due to the differentiation produced on the mammary cells. PMID: 25136563 Prolactin induces apoptosis of lactotropes PMID: 24859278 High Prolactin expression is associated with Streptozotocin diabetes. PMID: 24984282 insulin activates prolactin gene transcription by activating Elk-1 that recruits the NuA4 complex to the promoter. PMID: 24075908 PRL acts on ARC neurons to inhibit kisspeptin expression in female rats PMID: 24456164 serum levels may be involved in the homing events to mammary glands, probably helping antibody-secreting cells and protecting the gland during lactation development PMID: 23904563 Prolactin inhibits apoptosis in chondrocytes in response to a mixture of proinflammatory cytokines. PMID: 23908112 Our data confirmed the regulatory role of dopamine, serotonin, and TRH on PRL secretion, however, the interaction between these and glutamatergic systems was not confirmed. PMID: 23641787 Data from 2 hepatic insufficiency models suggest that pituitary expression of Prl and estrogen receptor alpha is up-regulated in this state, positively correlating with increase in serum 17beta-estradiol level; data show gastro-hepato-pituitary axis. PMID: 22843122 The results indicate that under prolonged duration of a daily melatonin signal, rat anterior pituitary prolactin synthesis and release are depressed, together with significant changes in the redox and circadian mechanisms controlling them. PMID: 22891630 results show that the effect of centrally injected allopreganolone over reproductive function could be due to a centrally originated LH mediated effect over ovarian function that affects luteal regression, through the inhibition of apoptosis and stimulation of progesterone and prolactin release PMID: 22674474 Lactotroph nonselective cation channels, presumably belonging to the TRPC family, contribute to the background depolarizing conductance and firing of action potentials with consequent prolactin release. PMID: 22480423 Data suggest that the resolution of an inflammatory response is associated with dramatic activation of the prolactin (PRL) gene promoter in the myeloid lineage. PMID: 22495675 E(2) may act as a modulator of the prolactin secretory response induced by TRH through membrane estrogen receptors, with the contribution by PI3K/Akt pathway activation. PMID: 22354782 The results show that PRL expression and cell proliferation are controlled in part by CEBPD. PMID: 21980073 Gonadotrophs are the major source of Nrg1 in the normal anterior pituitary and Nrg1 may function as a paracrine/juxtacrine regulator of PRL secretion. PMID: 21919974 Data suggest that prolactin is involved in regulation of prolactin receptor expression and maintenance of physiological cell renewal in anterior pituitary. PMID: 22094470 Data suggest that inflammation leads to accumulation of endogenous prolactin in female and male rats, and that prolactin acts as an inflammatory mediator at different time points for female and intact male rats. PMID: 21777304 Prolactin inhibition during late lactation programs renal function damage in adult offspring. PMID: 21823059 Estradiol regulates dopamine-activataed GIRK channel activity in pituitary lactotrophs, regulating prolactin release during the estrous cycle. PMID: 21653876 Integrity of the pelvic nerve is necessary for the systemic oxytocin induction of the PRL secretory rhythm in ovariectomized rats. PMID: 21677274 NONO and SFPQ were functionally involved in circadian Prl transcription since overexpression of both proteins greatly reduced Prl promoter activity (P<0.001) and disrupted its circadian pattern. PMID: 21507896 The anterior pituitary production of 16 kDa prolactin is variable along the estrous cycle and increased by estrogens. PMID: 21760910 Complex interactions between Ahr and Esr alter Prl and luteinizing hormone (LH) synthesis by direct actions in lactotropes and gonadotropes. PMID: 21187122 Results suggest that bone morphogenetic proteins elicit differential actions in the regulation of prolactin release dependent on cellular cAMP-PKA activity. PMID: 20970474 PREB can function as a transcriptional regulator of PRL promoter activity and might be involved in TRH-induced PRL gene transcription PMID: 20960102 Results suggest a role for dopamine in the generation of the oestrous prolactin surge. PMID: 20722974 Prolactin diminishes the damaging actions of excitotoxicity in the kainate model of epilepsy. PMID: 20570717 Data show that inactivation of tyrosine hydroxylase in hypothalamic neuroendocrine dopamine neurons is required for suckling-induced prolactin and ACTH responses. PMID: 20170714 Results demonstrate clearly that certain circadian elements binding to the E-box133 site are required for episodes of PRL mRNA expression. PMID: 20215567 Prolactin gene expression data suggest that pituitary tissue comprises a series of cell ensembles, which individually display a variety of patterns of short-term stochastic behaviour, but together yield long-range and long-term coordinated behaviour. PMID: 20130141 results indicate that specific effects upon male rat lactotropes may be exerted by PRL variants released from anterior pituitary glands of lactating and non-lactating rats PMID: 19590175 At 5 h after progesterone (P(4)) treatment, tyrosine hydroxylase activity and phosphorylation state declined coincident with an increase in plasma prolactin in both P(4)-treated morning and afternoon groups. PMID: 19945993 PRL directly enhanced the transcellular and paracellular calcium transport in the rat cecum through the nongenomic signaling pathways involving PI3K, PKC, and ROCK. PMID: 19449156 Review: evidence demonstrating PRL synthesis by different subtypes of immune cells from humans, mice and rats, describe the regulation of PRL gene expression in human lymphocytes, and discuss the functions of PRL made by immune cells. PMID: 11721692 Review: Effects of prolactin on signal transduction and gene expression: possible relevance for systemic lupus erythematosus. PMID: 11721698 Review: effects of changing the ratio of these two forms in maternal PRL on gamma delta T cell development in rat pups in utero PMID: 11721700 physiological prolactin secretion response to stress depends on the renin--angiotensin system PMID: 11888852 Inverse control of prolactin and growth hormone gene expression: effect of thyroliberin on transcription and RNA stabilization. PMID: 11892801

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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.