SARS-CoV-2 RdRP Protein (sf9, His, Strep)

The multifunctional SARS-CoV-2 PP1ab protein is essential for viral RNA transcription and replication, utilizing proteases for multi-protein cleavage. It inhibits host translation by binding to the 40S subunit and blocks ribosomal mRNA entry channels, thereby hindering the antiviral response. RdRP Protein, Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2) (Sf9, His, Strep) is the recombinant virus-derived RdRP, expressed by Sf9 insect cells, with Strep, His labeled tag.

The SARS-CoV-2 PP1ab protein is a multifunctional component crucial for the transcription and replication of viral RNAs, housing the proteinases responsible for polyprotein cleavages. This protein plays a pivotal role in inhibiting host translation by associating with the open head conformation of the 40S subunit, and its C-terminus obstructs the ribosomal mRNA entry tunnel, thereby impeding the antiviral response triggered by innate immunity or interferons. The formation of the nsp1-40S ribosome complex leads to an endonucleolytic cleavage near the 5'UTR of host mRNAs, facilitating their degradation. Notably, viral mRNAs exhibit greater resistance to the nsp1-mediated inhibition of translation due to their 5'-end leader sequence. This multifaceted functionality underscores the strategic role of SARS-CoV-2 PP1ab in manipulating host cellular processes for the benefit of viral replication and evasion of host defenses.

Virus

Sf9 insect cells

Strep;His

P0DTD1 (S1-Q932, nsp12 )

/

Partial

<1 EU/μg, determined by LAL method.