Recombinant Human NPR2 Protein

Name: Recombinant Human NPR2 Protein
Brand: Beta LifeScience
SKU: BL-1162SG
Availability: InStock

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Tag	GST
Host Species	Human
Accession	NM_003995
Synonym	AMDM; ANPB; ANPRB; GUC2B; GUCY2B; NPRB; NPRBi
Background	NPR2 encodes natriuretic peptide receptor B, one of two integral membrane receptors for natriuretic peptides which produce cytoplasmic cyclic GMP from GTP on binding its extracellular ligand, C-type natriuretic peptide (1).The granulosa cell ligand NPPC and its receptor NPR2 in cumulus cells prevent precocious meiotic maturation which is critical for maturation and ovulation synchrony and for normal female fertility. NPR2 is critical for the development of both bone and female reproductive organs (2).
Description	Recombinant human NPR2 (479-end) was produced by baculovirus in Sf9 insect cells, fused with a GST tag at N-terminus. This protein is purified with our unique purification methods.
Source	Sf9 insect cells
AA Sequence	479a.a.-end
Molecular Weight	86 kDa
Purity	For specific purity information on a given lot, see related COA.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability	The recombinant protein is stable for up to 12 months at -70°C
Usage	For Research Use Only
Storage	Recombinant Human NPR2 Protein should be stored should be stored at < -70°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Receptor for the C-type natriuretic peptide NPPC/CNP hormone. Has guanylate cyclase activity upon binding of its ligand. May play a role in the regulation of skeletal growth.
Subcellular Location	Cell membrane; Single-pass type I membrane protein.
Protein Families	Adenylyl cyclase class-4/guanylyl cyclase family
Database References	HGNC: 7944 OMIM: 108961 KEGG: hsa:4882 STRING: 9606.ENSP00000341083 UniGene: PMID: 27283501 in 4 Indian families with acromesomelic dysplasia, type Maroteaux, 4 homozygous mutations in four different families were identified; these include 3 novel mutations including a deletion frameshift mutation (p.Cys586Ter), one nonsense mutation (p.Arg479Ter), one missense mutation (p.Val187Asp) and one reported missense mutation (p.Tyr338Cys) PMID: 27994189 Heterozygous mutation in NPR2 gene is associated with short stature. PMID: 27941173 Mutations in three genes (GDF5, NPR2, BMPR1B) have been reported to cause different forms of acromesomelic dysplasia PMID: 26926249 IL1R2 hypomethylation and androgen receptor hypermethylation may constitute an important determinant of disease severity, whereas NPR2 hypomethylation and SP140 hypermethylation may provide a biomarker for vulnerability to excessive daytime sleepiness in Obstructive Sleep Apnea PMID: 26888452 Loss-of-function mutations of the NPR2 gene is associated with acromesomelic dysplasia, type maroteaux. PMID: 26567084 Heterozygous mutations in natriuretic peptide receptor-B (NPR2) gene as a cause of short stature PMID: 25703509 NPR2 mutations account for approximately 3% of patients with disproportionate short stature and/or clinical or radiographic indicators of SHOX deficiency and in whom no SHOX defect has been identified. PMID: 26075495 3 consanguineous families segregating Acromesomelic dysplasia Maroteaux type in an autosomal recessive manner studied. Linkage in the families was established to the NPR2 gene on chromosome 9p12-21. Sequence analysis revealed 2 novel missense variants (p.Arg601Ser; p.Arg749Trp) in 2 families and a previously reported splice site variant (c.2986+2T>G) in the third family. PMID: 25959430 Overgrowth syndrome associated with a gain-of-function mutation of the natriuretic peptide receptor 2 (NPR2) gene. PMID: 24259409 Identification of heterozygous dominant negative NPR2 mutations in 2% of Japanese patients with short stature. PMID: 24471569 KIdney NPR2 protein quantity is significantly impacted by genetic variation. PMID: 23835779 study concludes V883M mutation increases maximal velocity in absence of C-type natriuretic peptide (CNP), eliminates requirement for ATP in the CNP-dependent Km reduction and disrupts normal inactivation process; established a molecular mechanism for how an amino acid substitution in GC-B activates the enzyme, which results in abnormally long and fragile bones PMID: 23827346 In transgenic mice, complete absence of Npr2 activity prohibits the bifurcation of cranial sensory axons. PMID: 24431432 Although no novel phosphorylation sites that influenced the suppression of guanylate cyclase-B were identified, experiments revealed that mutations in Tyr808 markedly enhanced GC-B activity. PMID: 23586811 We identified heterozygous NPR2 mutations in 6% of patients initially classified as idiopathic short stature. Affected patients have mild and variable degrees of short stature without a distinct phenotype. PMID: 24001744 The extracellular domain of human GC-B folds independently of the remainder of the protein. PMID: 19108585 An overgrowth disorder associated with excessive production of cGMP due to a gain-of-function mutation of the natriuretic peptide receptor 2 gene. PMID: 22870295 Patients with BNP on admission greater than 150/pg/ml have higher probability of death in follow up. PMID: 22633662 Two novel missense mutations in the gene NPR2 were identified six consanguineous families of Pakistani origin. The presence of the same mutation (p. T907M) and haplotype in five families (A, B, C, D, E) is suggestive of a founder effect. PMID: 22691581 NPR2 expression in normal human fetal and adult pituitaries and adenomatous pituitary tissue suggests a role for these receptors in both pituitary development and oncogenesis. PMID: 22645228 GC-B activity is increased in non-myocytes from failing human ventricles, possibly as a result of increased fibrosis. PMID: 22133375 results provide evidence for a potential causal role of the B-type natriuretic peptide system in the aetiology of type 2 diabetes PMID: 22039354 Data show that serum B-type natriuretic peptide strongly correlates with new-onset heart failure development at the optimal cut-off value of 175 pg/mL. PMID: 20600420 These studies showed the presence of NPR-A and NPR-B (mRNAs and protein) in human corneal epithelial tissue. PMID: 20664698 A polymorphism in natriuretic peptide receptor 2 influences the susceptibility to idiopathic dilated cardiomyopathy in a Chinese cohort. PMID: 20123316 Results show that VILIP-1 regulates the cell surface localization of natriuretic peptide receptor B. PMID: 20079378 NPR-B is highly expressed in glomeruli and proximal tubules, whereas NPR-Bi(the splice form) shows strong signals in the distal nephron PMID: 12709393 a marker for left ventricular dysfunction in diabetic patients. PMID: 14988324 Mutations in the transmembrane natriuretic peptide receptor NPR-B impair skeletal growth and cause acromesomelic dysplasia, type Maroteaux PMID: 15146390 The 5' terminus of the hNPR-B gene transcript is ~732 base pairs upstream from the presumed translation start site. Its activity is dominated by a single cluster of Sp1-binding elements in the proximal 5' flanking sequence of the gene. PMID: 15262909 hyperosmotic and lysophosphatidic acid-dependent inhibition of NPRB is mediated by calcium-dependent phosphorylation PMID: 15371450 Study focus on the role of NPR-B and its ligand C-type natriuretic peptide in cardiovascular physiology and disease. PMID: 17429599 intact kinase homology domain of NPR-B is essential for skeletal development PMID: 17652215 Defective cellular trafficking of NPR-B resulted from missense mutation is associated with acromesomelic dysplasia-type Maroteaux. PMID: 18945719 BNP level on arrival in the intensive care unit may support early diagnosis and allow optimal management of heart failure after aortic valve replacement PMID: 19167912 It appears that subjects homozygous for C allele at position 381 of the BNP precursor gene promoter are more prone to develop atherosclerotic lesions in renal arteries. PMID: 19413180 protein structure: ligand binding domains PMID: 11556325

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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.