Recombinant Human Atrial Natriuretic Peptide Receptor 1 (NPR1) Protein (His-SUMO)

Name: Recombinant Human Atrial Natriuretic Peptide Receptor 1 (NPR1) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-03356P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) NPR1.

Collections: All products, High-quality recombinant proteins, Other 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 Atrial Natriuretic Peptide Receptor 1 (NPR1) Protein (His-SUMO) is produced by our E.coli expression system. This is a extracellular protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P16066
Target Symbol	NPR1
Synonyms	ANP-A; ANPa; ANPR-A; ANPRA; ANPRA_HUMAN; Atrial natriuretic peptide A type receptor; Atrial natriuretic peptide receptor 1; Atrial natriuretic peptide receptor A; Atrial natriuretic peptide receptor type A; Atrionatriuretic peptide receptor A; GC A; GC-A; Guanylate cyclase A; Guanylate cyclase; GUC2A; GUCY2A; Natriuretic peptide A type receptor; Natriuretic Peptide Receptor A; Natriuretic peptide receptor A/guanylate cyclase A; NPR-A; NPR1; NPRA
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	GNLTVAVVLPLANTSYPWSWARVGPAVELALAQVKARPDLLPGWTVRTVLGSSENALGVCSDTAAPLAAVDLKWEHNPAVFLGPGCVYAAAPVGRFTAHWRVPLLTAGAPALGFGVKDEYALTTRAGPSYAKLGDFVAALHRRLGWERQALMLYAYRPGDEEHCFFLVEGLFMRVRDRLNITVDHLEFAEDDLSHYTRLLRTMPRKGRVIYICSSPDAFRTLMLLALEAGLCGEDYVFFHLDIFGQSLQGGQGPAPRRPWERGDGQDVSARQAFQAAKIITYKDPDNPEYLEFLKQLKHLAYEQFNFTMEDGLVNTIPASFHDGLLLYIQAVTETLAHGGTVTDGENITQRMWNRSFQGVTGYLKIDSSGDRETDFSLWDMDPENGAFRVVLNYNGTSQELVAVSGRKLNWPLGYPPPDIPKCGFDNEDPACNQDHLSTLE
Expression Range	33-473aa
Protein Length	Extracellular Domain
Mol. Weight	64.9kDa
Research Area	Cardiovascular
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 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	Receptor for the atrial natriuretic peptide NPPA/ANP and the brain natriuretic peptide NPPB/BNP which are potent vasoactive hormones playing a key role in cardiovascular homeostasis. Has guanylate cyclase activity upon binding of the ligand.
Subcellular Location	Membrane; Single-pass type I membrane protein.
Protein Families	Adenylyl cyclase class-4/guanylyl cyclase family
Database References	HGNC: 7943 OMIM: 108960 KEGG: hsa:4881 STRING: 9606.ENSP00000357669 UniGene: PMID: 28765884 The results indicate that the inhibition of NPRA suppresses gastric cancer development and targeting NPRA may represent a promising strategy for the treatment of gastric cancer. PMID: 27634171 Data suggest that signaling via ANP/ANPR (atrial natriuretic factor/ANP receptor) in vascular endothelial cells activates PAK4 (p21-activated kinase 4) and CCM2 (cerebral cavernous malformation 2 protein), resulting in phosphorylation of MLC (myosin light chain), cytoskeletal reorganization, and cell spreading; kinase homology domain of ANPRA (guanylyl cyclase-A) activates downstream targets of ANP/ANPR signaling. PMID: 28432261 After ligand binding, NPRA is rapidly internalized and trafficked from the cell surface into endosomes, Res and lysosomes, with concurrent generation of intracellular cyclic GMP in HEK-293 cells. PMID: 26374856 Data suggest up-regulation of NPRA in skeletal muscle (SM) correlates with whole-body insulin sensitivity; NPRA is down-regulated in SM in obese subjects compared to normal controls; NPRA in SM is up-regulated in response to diet-induced weight loss. PMID: 26253614 In this review we highlight the mechanisms by which NPR-A affects signaling pathways involved in inflammation and cancer, and we discuss its potential as a novel target in inflammation, cancer, and cancer-related inflammation PMID: 25955817 NPRA was detected in E11.5 cardiac progenitor cells. PMID: 25631869 Cardiac fibrosis and the endogenous natriuretic peptide system were evaluated in end-stage heart failure to assess the anti-fibrotic actions of the dual GC-A/-B activator. PMID: 25117468 High NPR1 expression is associated with esophageal squamous cell carcinomas. PMID: 24885858 Molecular dynamics analysis indicated decreases in the values of Van der Waals, electrostatic energy and potential energy of NPRB/Vasonatrin peptide compared to NPRA/Vasonatrin peptide. PMID: 24699414 ACNP stimulated both human natriuretic peptide receptors (NPRs), NPRA and NPRB, as potent as their native ligands in receptor transfected cells. PMID: 23186809 Guanylyl cyclases A and B are asymmetric dimers that are allosterically activated by ATP binding to the catalytic domain. PMID: 22949736 human ventricular cardiomyocytes express low levels of GC-A and GC-A in cardiomyocytes from failing human hearts is refractory to ANP stimulation. PMID: 22133375 Results demonstrate the opposite effects of NPR-A and NPR-C in LPS-mediated endothelial permeability and lung injury. PMID: 22001395 Cellular exposure to Go6976 reduced basal and natriuretic peptide-dependent, but not detergent-dependent, GC-A and GC-B activity. PMID: 21366551 Go6976 reduces GTP binding to the catalytic site of GC-A and GC-B and that ATP increases the magnitude of the inhibition. PMID: 21828054 Midregional pro-A-type natriuretic peptide has a comparable accuracy to brain natriuretic peptide BNP for evaluation of cardiocirculatory exercise limitation. PMID: 20034689 NPRA promotes prostate cancer development in part by regulating macrophage migration inhibitory factor PMID: 21586128 review attempts to provide insights and to delineate the current concepts in the field of functional genomics and signaling of GC-A/NPRA in hypertension and cardiovascular disease states at the molecular level PMID: 21375691 we identified and characterized new phosphorylation sites in GC-A and GC-B and provide the first evidence of phosphorylation sites within human guanylyl cyclases. PMID: 20977274 The SS genotype of the AGT gene was related with an increased risk for 3-vessel CAD PMID: 20529973 kinetics of internalization, trafficking, and down-regulation of recombinant guanylyl cyclase/natriuretic peptide receptor-A (NPRA) PMID: 11704663 unlikely that NPR1 is the same as the MCKD1 gene, mutations in which cause the adult form of medullary cystic kidney disease type 1; however, it is presently unknown whether it plays a disease modifying role PMID: 11851379 This gene codes for natriuretic peptide receptor A, which mediates natriuretic, diuretic, and vasorelaxing actions of the natriuretic peptides. PMID: 12483301 The "deletion 15129" variant might participate in the functional impairment of natriuretic peptide system defining and increased genetic susceptibility to hypertension. PMID: 12506509 activation stabilizes a membrane-distal dimer interface PMID: 12547834 Human dendritic cells, but not monocytes, express functional ANP receptor GC-A at both mRNA and protein levels. PMID: 12794112 NPRA-PKG association may have a role in compartmentation of cGMP-mediated signaling and regulation of receptor sensitivity PMID: 12855709 The novel Npr1 gene 3C variant and the Npr3 gene C(-55) allele are associated with hypertensive family history PMID: 12872042 the M341I missense mutation is associated with risk of myocardial infarct (MI) and may be a genetic marker of MI PMID: 14646971 NPR-A and NPR-B are desensitized in cells in which they are not internalized. PMID: 15459247 discussion of experimental insights into the mechanisms that cells utilize in modulating the delivery and metabolic processing of ligand-bound NPRA into the cell interior [review] PMID: 15911067 discussion of the functional significance of the promoter region of Npr1 gene and its transcriptional regulation [review] PMID: 15911069 ATP does not activate NPRA and NPRB as has been repeatedly reported. Instead, ATP increases activity primarily by maintaining proper receptor phosphorylation status but also serves a previously unappreciated enzyme stabilizing function. PMID: 15911610 interaction of atrial natriuretic peptide with natriuretic peptide receptor-A modulates the binding of ATP to the kinase homology domain PMID: 16262696 NPR-A protein localized to cardiomyocytes, endocardial endothelial cells, and smooth muscle of intramyocardial vessels; downregulation in the density of NPR-A in heart and coronary was observed in artery of patients with ischemic heart disease PMID: 16778132 Data suggest that natriuretic peptide receptor A (NPR-A) interacts with fibronectin to enhance brain natriuretic peptide (BNP) activation of cyclic GMP and that a small NPR-A-specific RGD peptide augments this action of BNP. PMID: 16986166 In patients with Dukes stage C/D colorectal cancer, the Cox Proportional Hazard Model analysis demonstrated a significant association between increased patient survival and low expression of ITGB2 (p = 0.011) and NPR1 (p = 0.023) genes. PMID: 18306933 Real-time PCR revealed that large adipocytes expressed higher mRNA levels of NPRA, and binding studies showed that large adipocytes expressed more NPR-A on the membrane than small adipocytes. PMID: 18383440 The "4-minus" haplotype of the NPR-A receptor gene is associated with high NT-proBNP values and is a genetic determinant of the interindividual variability in the BNP system in healthy individuals but probably not in patients with cardiovascular disease. PMID: 18436476 In the present study conducted in a homogeneous Hellenic population, no associations between Angiotensinogen,angiotensin-converting enzyme, and NPRA gene polymorphisms and hypertension were found. PMID: 19126660 These results indicate that the ANP/GC-A system is involved in immune regulation through plasmacytoid dendritic cells in secondary lymphoid organs. PMID: 19563399

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.