Analytical Data
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Gene name
I614N
- Application
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Alternative Names
I614N；
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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
P19821
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Expression Region
293-832aa
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AA Sequence
ALEEAPWPPPEGAFVGFVLSRKEPMWADLLALAAARGGRVHRAPEPYKALRDLKEARGLLAKDLSVLALREGLGLPPGDDPMLLAYLLDPSNTTPEGVARRYGGEWTEEAGERAALSERLFANLWGRLEGEERLLWLYREVERPLSAVLAHMEATGVRLDVAYLRALSLEVAEEIARLEAEVFRLAGHPFNLNSRDQLERVLFDELGLPAIGKTEKTGKRSTSAAVLEALREAHPIVEKILQYRELTKLKSTYIDPLPDLIHPRTGRLHTRFNQTATATGRLSSSDPNLQNIPVRTPLGQRIRRAFIAEEGWLLVALDYSQNEIRVLAHLSGDENLIRVFQEGRDIHTETASWMFGVPREAVDPLMRRAAKTINFGVLYGMSAHRLSQELAIPYEEAQAFIERYFQSFPKVRAWIEKTLEEGRRRGYVETLFGRRRYVPDLEARVKSVREAAERMAFNMPVQGTAADLMKLAMVKLFPRLEEMGARMLLQVHDELVLEAPKERAEAVARLAKEVMEGVYPLAVPLEVEVGIGEDWLSAKE
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Molecular Weight
61.0 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 I614N recombinant protein is a variant that has gained significant attention in the field of virology, particularly in the study of SARS-CoV-2, the virus responsible for COVID-19. This research focuses on understanding the mutations that arise in the virus as it spreads, which can influence its transmissibility, virulence, and response to vaccines. The I614N mutation, specifically, has been observed to enhance the stability of the spike protein, which is critical for the virus's ability to infect host cells. Increased stability of the spike protein may lead to more efficient viral entry and infectivity. As researchers strive to develop effective vaccines and therapeutics, understanding the implications of such mutations is crucial, as they may affect vaccine efficacy or lead to the emergence of new variants that could evade existing immune responses. Consequently, studies on the I614N recombinant protein are essential for informing public health strategies and guiding the design of next-generation vaccines that can provide broad protection against diverse viral strains. By investigating the structural and functional characteristics of this variant, scientists aim to unravel its role in viral dynamics and its potential impact on the ongoing fight against COVID-19.
