Coronavirus NSP8 Proteins, cDNA Clones Research Reagents

Viral non-structural protein NSP8 forms a hexadecameric supercomplex with NSP7 that adopts a hollow cylinder-like structure. NSP7 and NSP8 heterodimers play a role in the stabilisation of NSP12 regions involved in RNA binding and are essential for a highly active NSP12 polymerase complex. NSP8 has N-terminal and C-terminal D/ExD/E conserved motifs. The N-terminal motif is critical for RNA polymerase activity as these residues are part of the Mg2-binding active site.

Coronavirus NSP8 Protein (1)

    Coronavirus NSP8 cDNA Clone (1)

    SARS-CoV-2

    In expression vector

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    Coronavirus NSP8 Background

    NSP8 is a nonstructural protein of coronavirus. NSP8 acts as a primase in RNA synthesis. NSP8 and NSP7 are essential co-factors of NSP12 (the catalytic subunit with RNA-dependent RNA polymerase activity) that can remarkably stimulate RdRp activity. The nsp12-nsp7-nsp8 subcomplex is defined as the minimal core component for mediating coronavirus RNA synthesis.

    Coronavirus NSP8 References

    • Qi Peng,et al.Structural and Biochemical Characterization of the nsp12-nsp7-nsp8 Core Polymerase Complex from SARS-CoV-2.Cell Reports.2020
    • Yan Gao,et al.Structure of the RNA-dependent RNA polymerase from COVID-19 virus.Science.2020
    • Purnima Kumar,et al.The nonstructural protein 8 (nsp8) of the SARS coronavirus interacts with its ORF6 accessory protein.Virology.2007

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