CstF-50 Polyclonal Antibody
Sizes: 50µl, 100µl
Catalogue Numbers: BS71939-50, BS71939-100
Product: Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Swiss-Prot: Q05048
Host: Rabbit
Reactivity: Human, Mouse, Rat
Applications: WB
All Applications: WB 1:500 - 1:2000
Background: 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.
Purification and Purity: The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Storage and Stability: Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze-thaw cycles.
Specificity: CstF-50 polyclonal antibody detects endogenous levels of CstF-50 protein.
Bioworld Molecular Weight: 50kDa
Note: For research use only, not for use in diagnostic procedure.
Extra Notes: Western Blot analysis of extracts of various cell lines, using CSTF1 antibody at 1:1000 dilution.
Alternative Name: Cleavage stimulation factor subunit 1; CF-1 50 kDa subunit; Cleavage stimulation factor 50 kDa subunit; CSTF 50 kDa subunit; CstF-50; CstF50; CSTF1
Immunogen: Recombinant protein of human CSTF1
Conjugate: Unconjugated
Modification: Unmodified