Analytical Data
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Gene name
M2
- Application
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Alternative Names
Proton channel protein M2
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Species
Influenza A virus
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A0A2R3YRM7
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Expression Region
1-97aa
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Molecular Weight
18.6kDa
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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
M2 protein, found in influenza A viruses, is a vital component in the viral life cycle, functioning primarily as an ion channel. It plays a critical role in viral uncoating and replication by facilitating the transport of protons into the virus, thereby enabling the release of viral RNA into the host cell's cytoplasm. The study of M2 protein has gained significant attention due to its potential as a target for antiviral therapies, especially in light of increasing resistance to existing antiviral drugs like amantadine and rimantadine. Researchers have focused on understanding the structure, function, and dynamics of M2, utilizing techniques such as X-ray crystallography, cryo-electron microscopy, and molecular dynamics simulations. This research not only sheds light on the mechanisms of viral pathogenesis but also paves the way for the design of new drugs that can effectively inhibit M2's activity. Additionally, the evolving nature of influenza viruses necessitates continuous monitoring and study of M2, as mutations may impact its functionality and resistance profiles. Overall, the ongoing exploration of M2 protein is crucial for developing innovative strategies to combat influenza infections and enhance global health security.
