CSTF1 is similar to mammalian G protein beta subunits and contains transducin-like repeats . These repeats are involved in protein-protein interactions, which are critical for the function of CSTF1 in the cleavage and polyadenylation complex. The protein is composed of several transcript variants with different 5’ untranslated regions (UTRs), but they all encode the same protein .
The recombinant form of CSTF1 is produced using Escherichia coli (E. coli) as the expression system . This recombinant protein is often tagged with a His-tag at the C-terminus to facilitate purification and detection . The recombinant CSTF1 protein is typically used in research applications, such as Western Blot (WB) or imaging assays, rather than functional studies due to its denatured state .
Recombinant CSTF1 is highly purified, with a purity greater than 90% as determined by SDS-PAGE . It is supplied in a liquid formulation containing 20 mM Tris-HCl buffer (pH 8.0), 20% glycerol, 0.1 M NaCl, and 2M urea . For storage, it is recommended to keep the protein at 4°C for short-term use and at -20°C for long-term storage, avoiding freeze-thaw cycles to maintain its stability .
CSTF1 plays a vital role in the regulation of gene expression by ensuring the proper processing of pre-mRNAs. Its involvement in the cleavage and polyadenylation of pre-mRNAs makes it a significant target for research in understanding gene expression mechanisms and potential therapeutic interventions.
For more detailed information, you can refer to the sources here and here.