Analytical Data
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Gene name
NPR1/NPRA
- Application
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Alternative Names
ANPRA; ANPa; GUC2A; GUCY2A; NPR-A; Guanylate Cyclase A; Atrionatriuretic Peptide Receptor A; Atrial natriuretic peptide receptor type A
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P16066
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Expression Region
Gly33~Glu473
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Molecular Weight
70kDa
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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 (NPR-A) and NPRA are receptor proteins belonging to the natriuretic peptide receptor family, primarily involved in cardiovascular regulation and fluid homeostasis. NPR1 acts as a receptor for atrial natriuretic peptide (ANP) and brain natriuretic peptide (BNP), facilitating signaling pathways that promote vasodilation, natriuresis, and diuresis, which are crucial for controlling blood pressure and cardiovascular health. Research on NPR1/NPRA recombinant proteins has gained traction due to their potential therapeutic implications in treating various cardiovascular diseases, including heart failure and hypertension. By studying these receptors through recombinant protein technology, scientists aim to better understand their functional mechanisms, signaling pathways, and interactions with their ligands. This knowledge could lead to the development of novel drugs that target NPR1/NPRA signaling, offering new avenues for managing cardiovascular disorders. Additionally, understanding the structural and functional characteristics of these proteins can enhance our comprehension of their roles in physiological and pathological conditions, providing deeper insights into heart function and fluid balance in the body.
