Polyadenylation of mRNA precursors is a two-step reaction that requires multiple protein factors. The first step, endonucleolytic cleavage of polyadenylation substrates, requires CstF (cleavage stimulation factor), a heterotrimer that is composed of three distinct subunits of 77, 64 and 50 kDa. Heterotrimeric CstF recognizes GU and U-rich sequences located downstream of the polyadenylation site on RNA. The 50 kDa CstF subunit shares extensive homology with mammalian G protein beta-subunits and has a transducin repeat domain, which is a 44 amino acid-long sequence that is repeated seven times. CstF-50 interacts with the nuclear protein BARD1 (BRCA1-associated RING domain protein) and inhibits polyadenylation in vitro. CstF-50 may also be responsible for the interaction of the heterotrimeric CstF complex with other polyadenylation and 3-end cleavage factors to form a stable complex on the pre-mRNA.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
IHC: 1:50~1:200
Application Notes:
CstF-50 (R3) polyclonal antibody detects endogenous levels of CstF-50 protein
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