Analytical Data
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Gene name
SARS2
- Application
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Alternative Names
SARS2；NucleoProtein
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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
Q9NP81
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Expression Region
35-518aa
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AA Sequence
TTEKRN RNLLYEYARE GYSALPQLDI ERFCACPEEA AHALELRKGE LRSADLPAII STWQELRQLQ EQIRSLEEEK AAVTEAVRAL LANQDSGEVQ QDPKYQGLRA RGREIRKELV HLYPREAQLE EQFYLQALKL PNQTHPDVPV GDESQARVLH MVGDKPVFSF QPRGHLEIGE KLDIIRQKRL SHVSGHRSYY LRGAGALLQH GLVNFTFNKL LRRGFTPMTV PDLLRGAVFE GCGMTPNANP SQIYNIDPAR FKDLNLAGTA EVGLAGYFMD HTVAFRDLPV RMVCSSTCYR AETNTGQEPR GLYRVHHFTK VEMFGVTGPG LEQSSQLLEE FLSLQMEILT ELGLHFRVLD MPTQELGLPA YRKFDIEAWM PGRGRFGEVT SASNCTDFQS RRLHIMFQTE AGELQFAHTV NATACAVPRL LIALLESNQQ KDGSVLVPPA LQSYLGTDRI TAPTHVPLQY IGPNQPRKPG LPGQPAVS
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Molecular Weight
58.2 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 SARS-CoV-2 recombinant proteins has gained significant importance in light of the COVID-19 pandemic, which is caused by the novel coronavirus SARS-CoV-2. Since its emergence in late 2019, understanding the structure and function of SARS-CoV-2 proteins has been crucial for developing effective vaccines and therapeutics. Recombinant proteins are synthesized in laboratory settings to mimic natural viral proteins, allowing researchers to investigate their roles in viral infection and immune response. Key proteins, such as the Spike (S) protein, play a vital role in the virus's ability to enter human cells, making them prime targets for vaccine development. By producing and characterizing these proteins, scientists can evaluate their immunogenicity, study potential antiviral agents, and enhance the design of diagnostic tools. The rapid advancement in genetic engineering techniques has facilitated the production of SARS-CoV-2 recombinant proteins, leading to a better understanding of viral pathogenesis and immunity. This research is not only vital for immediate responses to COVID-19 but also lays the groundwork for future antiviral strategies against other emerging infectious diseases. Through collaborative global efforts and innovative research approaches, the study of recombinant proteins is pivotal in addressing the ongoing pandemic and preparing for future viral threats.
