Analytical Data
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Gene name
E & M
- Application
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Alternative Names
E & M；M；Matrix Protein 1
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P03519
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Expression Region
1-229aa
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AA Sequence
MSSLKKILGLKGKGKKSKKLGIAPPPYEEDTSMEYAPSAPIDKSYFGVDEMDTYDPNQLRYEKFFFTVKMTVRSNRPFRTYSDVAAAVSHWDHMYIGMAGKRPFYKILAFLGSSNLKATPAVLADQGQPEYHTHCEGRAYLPHRMGKTPPMLNVPEHFRRPFNIGLYKGTIELTMTIYDDESLEAAPMIWDHFNSSKFSDFREKALMFGLIVEKKASGAWVLDSISHFK
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Molecular Weight
26.0 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
The study of E & M recombinant proteins has gained significant attention in recent years due to their potential applications in various fields, including medicine, biotechnology, and vaccine development. E (envelope) and M (membrane) proteins are critical components of viral structures, particularly in enveloped viruses such as the flavivirus family, which includes pathogens like Zika and dengue. Understanding the structure and function of these proteins can provide insights into viral pathogenesis and immune response. Recombinant protein technology enables the production of these proteins in laboratory settings, which is essential for the development of targeted therapies and diagnostic tools. By manipulating genetic sequences, researchers can produce E & M proteins in sufficient quantities and purity, allowing for detailed characterization and evaluation of their biological activity. Recent advances in structural biology and immunology have also fueled research in this area, helping scientists to design more effective vaccines that elicit robust immune responses. Furthermore, as emerging infectious diseases continue to pose global health threats, the importance of studying E & M recombinant proteins cannot be overstated, as they serve as vital targets for developing novel antiviral strategies and improving public health responses.
