Analytical Data
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Gene name
NPR1/NPRA
- Application
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Species
Cynomolgus
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Source
HEK293
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Tag
C-mFc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
XP_005541810
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Expression Region
G33-E473
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Protein Length
Partial
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Molecular Weight
80-110 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
NPR1, also known as NPRA (Natriuretic Peptide Receptor A), is a receptor that plays a crucial role in the cardiovascular system, particularly in mediating the effects of natriuretic peptides, which are important for regulating blood pressure, sodium homeostasis, and fluid balance. Research on recombinant NPR1/NPRA proteins has gained significant attention due to their potential therapeutic applications in treating heart failure, hypertension, and other cardiovascular diseases. The NPRA activation leads to intracellular signaling cascades that promote vasodilation and natriuresis, offering insights into innovative drug development strategies. Additionally, the study of NPR1/NPRA is critical for understanding its role in various pathophysiological conditions, including cardiac hypertrophy and fibrosis. Recombinant proteins enable researchers to investigate the structure-function relationship of NPR1/NPRA, identify binding sites, and explore the molecular mechanisms underlying its action. Furthermore, the development of NPR1/NPRA antagonists or agonists holds promise for novel intervention strategies in modulating the cardiovascular response. Thus, elucidating the complexities of NPR1/NPRA through recombinant protein studies is essential for advancing our understanding of cardiovascular biology and improving therapeutic outcomes in patients with related disorders.
