SARS-CoV-2 Nucleocapsid Protein (203/204: RG>KR mutant, His-tagged)
A purified, soluble, recombinant SARS-CoV-2 nucleocapsid protein, His-tagged
A purified, recombinant SARS-CoV-2 nucleocapsid protein (R203K–G204R).
This protein represents the nucleocapsid protein from the variant of the original SARS-CoV-2 strain, in which the arginine-glycine amino acids in position 203-204 have been substituted with lysine-arginine (203/204: RG>KR mutation).
Details (see spec sheet for more details)
- Host: E. coli
- Tag: minimal N-terminal six-histidine tagged (HHHHHHG)
- Purity: >95%, assessed by SDS-PAGE.
- Formulation: Aqueous solution flash frozen at -80 °C
- Quantities available: 1 mg, 10 mg & 100 mg. Multiples may be ordered.
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(Note: Amino acids 9-426 of the sequence above matches residues 2-419 of SARS-CoV-2 Nucleocapsid protein GenBank entry QIQ08827)
The coronavirus nucleocapsid (N) protein has a structural role, binding to the viral RNA and forming the nucleocapsid. The N protein is highly immunogenic and abundantly expressed during infection which makes it an important marker in diagnostic assays for COVID-19. Recombinant nucleocapsid proteins are commonly used in viral quantification assays and in ELISAs for detection of human antibodies against coronavirus.
Many isolates encode this variant, for a fuller list of identical protein sequences see https://www.ncbi.nlm.nih.gov/ipg/QIQ08827.1
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Delivery and checkout questions
A £20 packaging charge is added at checkout to cover handling costs.
For UK orders: recipients are asked to provide details of their intended use for the material and to provide a courier code to cover delivery of material.
For International orders: The University ships this material internationally using INCOTERMS EXW (ex-works). The recipient is responsible for arranging delivery, insurance and payment of customs charges.
SARS-CoV-2, nucleocapsid, protein, coronavirus, COVID, COVID-19, 2019-ncov, variant, mutant, 203-204, RG>KR, R203K, G204R, arginine-glycine, lysine-arginine
Further information on the research group may be found at:
swap_vertical_circlemode_editAuthors (1)Prof Jon Sayers
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