CPSF4 Antibody

Inhibition of the nuclear export of poly(A)-containing mRNAs caused by the influenza A virus NS1 protein requires its effector domain. The NS1 effector domain functionally interacts with the cellular 30 kDa subunit of cleavage and polyadenylation specific factor 4, an essential component of the 3' end processing machinery of cellular pre-mRNAs. In influenza virus-infected cells, the NS1 protein is physically associated with cleavage and polyadenylation specific factor 4, 30kD subunit. Binding of the NS1 protein to the 30 kDa protein in vitro prevents CPSF binding to the RNA substrate and inhibits 3' end cleavage and polyadenylation of host pre-mRNAs. Thus the NS1 protein selectively inhibits the nuclear export of cellular, and not viral, mRNAs. Multiple alternatively spliced transcript variants that encode different isoforms have been described for this gene.

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

We have publications tested in 1 confirmed species: Human.

We have publications tested in 1 application: WB.

Showing Publications 1 - 2 of 2.

Publications using NB100-79826	Applications	Species
Pieraccioli M, Caggiano C, Mignini L et al. The transcriptional terminator XRN2 and the RNA-binding protein Sam68 link alternative polyadenylation to cell cycle progression in prostate cancer Nature structural & molecular biology 2022-11-01 [PMID: 36344846] (WB, Human)	WB	Human
Li W, Noah JW, Noah DL et al. Alanine substitutions within a linker region of the influenza A virus non-structural protein 1 alter its subcellular localization and attenuate virus replication. J Gen Virol 2011-08-01 [PMID: 21508188]

Array NB100-79826

• CPSF4 Antibodies
• CPSF4 Lysate
• CPSF4 Proteins