Rat Atrial Natriuretic Peptide Receptor 1 (NPR1) CLIA Kit

Product specifications

CLIA Kits

Atrial Natriuretic Peptide Receptor 1 (NPR1)

Rat

Chemiluminescent

Quantitative

Sandwich

0.312 ng/ml - 20 ng/ml

< 0.106 ng/ml

Optimal dilutions/concentrations should be determined by the end user.

96 tests

5 × 96 tests

10 × 96 tests

Lyophilized

CLIA

Tissue homogenates and other biological fluids.

Shipped within 5-20 working days.

 Shipped at 4 °C. Upon receipt, store the kit according to the storage instruction in the kit's manual.

No

ANPa,NPRA,ANPRA,GUC2A,GUCY2A,Guanylate cyclase A,GC-A,Atrial natriuretic peptide receptor type A

CLIA Kits NPR1

RUO

The validity for this kit is at least 6 months. Up to 12 months validity can be provided on request.   This product is for research use only.   The range and sensitivity is subject to change. Please contact us for the latest product information. For accurate results, sample concentrations must be diluted to mid-range of the kit. If you require a specific range, please contact us in advance or write your request in your order comments.   Please note that our ELISA and CLIA kits are optimised for detection of native samples, rather than recombinant proteins. We are unable to guarantee detection of recombinant proteins, as they may have different sequences or tertiary structures to the native protein.

Descripción

NPR1 is a guanylate cyclase-linked receptor that binds atrial natriuretic peptide (ANP) and brain natriuretic peptide (BNP), mediating their effects on vascular homeostasis, natriuresis, and diuresis. Upon ligand binding, NPR1 undergoes conformational changes that activate its intracellular guanylyl cyclase domain, producing cyclic GMP (cGMP), a second messenger that regulates vasodilation, blood pressure, and renal salt excretion. NPR1 is primarily expressed in vascular endothelial cells, renal tubular cells, and cardiac tissue, where it plays a pivotal role in maintaining cardiovascular and renal function. Mutations or dysregulation of NPR1 are associated with hypertension, heart failure, and other cardiovascular disorders due to impaired natriuretic signaling. Structural analyses reveal that NPR1 consists of an extracellular ligand-binding domain, a transmembrane region, and an intracellular guanylyl cyclase domain, highlighting its complex regulatory mechanisms. NPR1 also interacts with protein kinases and phosphodiesterases, fine-tuning the cGMP signaling cascade. In addition to cardiovascular effects, NPR1 signaling influences adipose tissue metabolism and has been linked to lipid regulation and energy homeostasis. Emerging research suggests that NPR1 activation could be a therapeutic target for managing hypertension and heart failure by enhancing natriuretic peptide activity.

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