Non-structural protein 1/NS1 Protein, H1N1 (His)

Nonstructural protein 1/NS1 plays multiple roles in viral infection. It inhibits cellular pre-mRNA processing by binding to CPSF4 and PABPN1, disrupting normal 3' end processing and halting host protein synthesis. Non-structural protein 1/NS1 Protein, H1N1 (His) is the recombinant Virus-derived Non-structural protein 1/NS1 protein, expressed by E. coli , with N-His labeled tag. The total length of Non-structural protein 1/NS1 Protein, H1N1 (His) is 229 a.a., with molecular weight of ~29 kDa.

The Non-structural protein 1/NS1 serves as a multifaceted regulator during viral infection. It exerts control over post-transcriptional processing of cellular pre-mRNA by binding and inhibiting essential cellular proteins, specifically the 30 kDa cleavage and polyadenylation specificity factor/CPSF4 and the poly(A)-binding protein 2/PABPN1. This interference prevents the normal 3'-end processing of cellular pre-mRNAs, leading to the accumulation of unprocessed pre-mRNAs in the host nucleus, effectively shutting down cellular protein synthesis. NS1 also plays a crucial role in evading the cellular antiviral response by inhibiting TRIM25-mediated RIGI ubiquitination, disrupting the activation of type I interferon genes. Additionally, NS1 interferes with the integrated stress response (ISR) by blocking dsRNA binding by EIF2AK2/PKR, inhibiting stress granule formation, and facilitating viral replication. This multifunctional protein further interacts with various cellular components, including TRIM25, EIF2AK2/PKR, CPSF4, IVNS1ABP, and PABPN1, highlighting its intricate involvement in modulating host cell processes to favor viral replication.

Virus

E. coli

N-His

C8XP22 (D2-V230)

/

Approximately 29 kDa

Greater than 95% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.