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Your Position: Home > Protein > NSP16 & NSP10 > NS0-C51W3

SARS-CoV-2 (COVID-19) NSP16&NSP10 Heterodimer Protein, His Tag&Twin Strep Tag

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  • Synonym
    NSP16 & NSP10,nsp16 & nsp10
  • Source
    SARS-CoV-2 NSP16&NSP10 Heterodimer Protein, His Tag&Twin Strep Tag(NS0-C51W3) is expressed from E. coli cells. It contains AA Ser 1 - Asn 298 (NSP16) & Ala 1 - Gln 139 (NSP10) (Accession # YP_009725311.1 (NSP16) & YP_009725306.1 (NSP10)).
    Predicted N-terminus: Met (NSP16) & Met (NSP10)
  • Molecular Characterization
    NSP16 & NSP10 Structure

    SARS-CoV-2 NSP16&NSP10 Heterodimer Protein, His Tag&Twin Strep Tag is produced by co-expression of NSP16 and NSP10, has a calculated MW of 35.3 kDa (NSP16) and 18.3 kDa (NSP10). Subunit NSP16 is fused with a polyhistidine tag at the N-terminus and subunit NSP10 is fused with a Twin Strep tag at the N-terminus. The reducing (R) heterodimer protein migrates as 18-19 kDa and 35 kDa.

  • Endotoxin
    Less than 1.0 EU per μg by the LAL method.
  • Purity

    >90% as determined by SDS-PAGE.

  • Formulation

    Supplied as 0.2 μm filtered solution in PBS, pH7.4 with glycerol as protectant.

    Contact us for customized product form or formulation.

  • Shipping

    This product is supplied and shipped with dry ice, please inquire the shipping cost.

  • Storage

    Please avoid repeated freeze-thaw cycles.

    This product is stable after storage at:

    1. The product MUST be stored at -70°C or lower upon receipt;
    2. -70°C for 3 months under sterile conditions.
SDS-PAGE
NSP16 & NSP10 SDS-PAGE

SARS-CoV-2 NSP16&NSP10 Heterodimer Protein, His Tag&Twin Strep Tag on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 90%.

  • Background
    NSP10, Plays a pivotal role in viral transcription by stimulating both nsp14 3-5 exoribonuclease and 2-O-methyltransferase (NSP16) activities. Therefore plays an essential role in viral mRNAs cap methylation. 2-O-methyltransferase (NSP16) that mediates mRNA cap 2-O-ribose methylation to the 5-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system. Nsp10 forms a dodecamer and interacts with nsp14 and nsp16; these interactions enhance nsp14 and nsp16 enzymatic activities.
  • Clinical and Translational Updates

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Price(USD) : $400.00

Price(USD) : $2860.00

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