Component of the THO subcomplex of the TREX complex. The TREX complex specifically associates with spliced mRNA and not with unspliced pre-mRNA. It is recruited to spliced mRNAs by a transcription-independent mechanism. Binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing-and cap-dependent manner to a region near the 5 end of the mRNA where it functions in mRNA export. The recruitment occurs via an interaction between THOC4 and the cap-binding protein NCBP1. UAP56 functions as a bridge between THOC4 and the THO complex. The TREX complex is essential for the export of Kaposis sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. The recruitment of the TREX complex to the intronless viral mRNA occurs via an interaction between KSHV ORF57 protein and THOC4. Splice factor that is required for the first ATP-dependent step in spliceosome assembly and for the interaction of U2 snRNP with the branchpoint. It has both RNA-stimulated ATP binding/hydrolysis activity and ATP-dependent RNA unwinding activity. Even with the stimulation of RNA, the ATPase activity is weak. It can only hydrolyze ATP but not other NTPs. The RNA stimulation of ATPase activity does not have a strong preference for the sequence and length of the RNA. However, ssRNA stimulates the ATPase activity much more strongly than dsRNA. It can unwind 5 or 3 overhangs or blunt end RNA duplexes in vitro. The ATPase and helicase activities are not influenced by U2AF2 and THOC4.
Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
Target-Kategorie:
The synthetic peptide sequence used to generate the antibody AP8740b was selected from the C-term region of human BAT1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
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