Analytical Data
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Gene name
NEP
- Application
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Alternative Names
Non-structural protein 2
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Species
Influenza A virus
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A0A5S9BFN7
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Expression Region
1-121aa
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Molecular Weight
20.4kDa
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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
The study of NEP (Neutral Endopeptidase), a membrane-bound zinc-dependent metalloprotease, has gained significant attention in recent years due to its critical roles in various physiological and pathological processes. NEP is involved in the degradation of bioactive peptides, including neuropeptides, natriuretic peptides, and angiotensin, thus playing an essential role in regulating blood pressure, neurotransmission, and immune responses. Dysregulation of NEP activity has been implicated in various diseases, including cardiovascular disorders, neurodegenerative diseases, and cancer. The characterization of NEP's structure and function is vital for understanding its mechanism of action and therapeutic potential. Researchers have focused on NEP's enzymatic properties, substrate specificity, and the regulatory pathways that modulate its activity. Additionally, NEP is a promising target for drug development, with efforts directed towards designing NEP inhibitors and modulators that could enhance or inhibit its activity for therapeutic purposes. Advances in molecular biology and protein engineering techniques have facilitated the generation of NEP recombinant proteins, enabling in-depth studies of its functionality and interactions with different ligands, paving the way for innovative therapeutic strategies. Overall, NEP research holds promise for elucidating the complex roles of peptide signaling in health and disease, providing potential avenues for innovative treatments and interventions.
