Analytical Data
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Gene name
M2-1
- Application
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Alternative Names
Envelope-associated 22 kDa protein
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Species
strain B1
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Source
E. coli
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Tag
N- His & C- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O42050
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Expression Region
1-195aa
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Molecular Weight
25.5 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
M2-1 protein, a critical factor in the replication of viruses such as the influenza virus, has garnered significant attention in virology and molecular biology research. This protein is part of the M2 ion channel, which plays a pivotal role in the viral life cycle by regulating proton flow into the viral particle, thereby facilitating viral uncoating once inside the host cell. Understanding the structural and functional properties of the M2-1 protein is essential for the development of antiviral strategies, as it is involved in the modulation of viral RNA transcription and replication. Investigations into the M2-1 protein have also highlighted its potential as a target for vaccine development, given its integral role in the virus's pathogenic mechanisms. Moreover, recent studies employing advanced techniques such as X-ray crystallography and cryo-electron microscopy have provided insights into its conformation and interaction with other viral components. The ongoing research around M2-1 not only enhances our knowledge of viral biology but also aids in the design of novel therapeutic agents capable of inhibiting viral replication, thus contributing to public health efforts in combating influenza and related viral infections.
