Further Information
Cleavage and polyadenylation specificity factor subunit 4, Cleavage and polyadenylation specificity factor 30 kDa subunit, CPSF 30 kDa subunit, NS1 effector domain-binding protein 1, Neb-1, No arches homolog, CPSF4, CPSF30, NAR, NEB1
For WB starting dilution is: 1:1000
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.
- Twu, K.Y., et al. J. Virol. 81(15):8112-8121(2007)
- Oh, J.H., et al. Mamm. Genome 16(12):942-954(2005)
- Kaufmann, I., et al. EMBO J. 23(3):616-626(2004)
- de Vries, H., et al. EMBO J. 19(21):5895-5904(2000)
Supplied in PBS with 0.09% (W/V) sodium azide.
batch dependent
Unconjugated
Optimal dilutions/concentrations should be determined by the end user. The information provided is a guideline for product use. This product is for research use only.
Predicted species reactivity based on immunogen sequence: Bovine, Rat, Xenopus
This CPSF4 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 96-123 amino acids from the Central region of human CPSF4.
10898
Cleavage and polyadenylation specificity factor subunit 4
CPSF4
Homo sapiens
Liquid
PREDICTED MOLECULAR WEIGHT:
30 kDa
O95639
This antibody is purified through a protein A column, followed by peptide affinity purification.
O95639
Optimal dilutions for each application to be determined by the researcher.