Analytical Data
-
Gene name
SARS
- Application
-
Alternative Names
N;NucleoProtein
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P49591
-
Expression Region
1-514aa
-
AA Sequence
MVLDLDLFRVDKGGDPALIRETQEKRFKDPGLVDQLVKADSEWRRCRFRADNLNKLKNLCSKTIGEKMKKKEPVGDDESVPENVLSFDDLTADALANLKVSQIKKVRLLIDEAILKCDAERIKLEAERFENLREIGNLLHPSVPISNDEDVDNKVERIWGDCTVRKKYSHVDLVVMVDGFEGEKGAVVAGSRGYFLKGVLVFLEQALIQYALRTLGSRGYIPIYTPFFMRKEVMQEVAQLSQFDEELYKVIGKGSEKSDDNSYDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHGRDTRGIFRVHQFEKIEQFVYSSPHDNKSWEMFEEMITTAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDYQARRLRIRYGQTKKMMDKVEFVHMLNATMCATTRTICAILENYQTEKGITVPEKLKEFMPPGLQELIPFVKPAPIEQEPSKKQKKQHEGSKKKAAARDVTLENRLQNMEVTDA
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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 recombinant proteins emerged as a critical area of research following the outbreak of Severe Acute Respiratory Syndrome (SARS) in 2002-2003, caused by the SARS coronavirus (SARS-CoV). This virus prompted global health concerns and highlighted the need for effective diagnostics, treatments, and vaccines. Recombinant proteins, which are artificially created through the expression of specific genes in host cells, play a vital role in understanding the virus's structure and function, particularly its spike (S) protein, which is crucial for viral entry into host cells. Researchers focused on producing these proteins to develop serological assays for detecting SARS-CoV antibodies and to elucidate immune responses. Furthermore, SARS recombinant proteins serve as essential components in vaccine development and therapeutic interventions, offering insights into potential cross-reactivity with other coronaviruses, such as MERS-CoV and the novel SARS-CoV-2. Understanding the antigenic properties and functional mechanisms of these recombinant proteins is not only vital for SARS research but also essential for preparing for future coronavirus outbreaks, ultimately enhancing global pandemic preparedness and response strategies.
