| Product Name | CPSF4, 1-244aa, Human |
|---|---|
| Description | 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 CPSF4 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. Recombinant human CPSF4 protein, fused to His-tag at N-terminus, was expressed in E.coli. |
| Synonyms | cleavage and polyadenylation specific factor 4,30kDa, CPSF30, NAR, NEB1 |
| Host | E. coli |
| Molecular Weight | 23.1 kDa (201aa) |
| Amino Acid Sequence | MGSSHHHHHH SSGLVPRGSH MGSMQEIIAS VDHIKFDLEI AVEQQLGAQP LPFPGMDKSG AAVCEFFLKA ACGKGGMCPF RHISGEKTVV CKHWLRGLCK KGDQCEFLHE YDMTKMPECY FYSKFGECSN KECPFLHIDP ESKIKDCPWY DRGFCKHGPL CRHRHTRRVI CVNYLVGFCP EGPSCKFMHP RFELPMGTTE QPPLPQQTQP PAKQRTPQVI GVMQSQNSSA GNRGPRPLEQ VTCYKCGEKG HYANRCTKGH LAFLSGQ |
| Tag | His-tag |
| Reactivity | Human |
| Applications | SDS-PAGE |
| Form | Liquid, in 20mM Tris-HCl buffer (pH 8.0) containing 0.4M urea, 10% glycerol |
| Concentration | 1 mg/ml (determined by Bradford assay) |
| Purity | > 85% by SDS-PAGE |
| Storage | Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -2°C or -7°C. Avoid repeated freezing and thawing cycles. |
| References | Jenny,A., et al. (1994) Mol. Cell. Biol. 14 (12), 8183-8190 Barabino,S.M., et al. (1997) Nephrol Genes Dev. 11 (13), 1703-1716 |
| Background | 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 CPSF4 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. Recombinant human CPSF4 protein, fused to His-tag at N-terminus, was expressed in E.coli. |
| Supplier | ARP |
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