SRSF3 Antibody #51039

Serine/arginine-rich splicing factor 3 (SRSF3), also known as SRP20, is a member of the highly conserved family of SR proteins responsible for splicing regulation (1,2). SRSF3 promotes exon inclusion by enhancing the recognition of weak splice acceptor sites, a function that also regulates its own mRNA by including exon 4. This function is antagonized by another SR family member, SRSF1 (3). SRSF3 can be shuttled in and out of the cytoplasm, where it plays a role in mRNA export along with SRSF7 (3,4). SRSF3 and SRSF7 have been shown to exert opposing effects on 3’UTR length by recruiting various proteins upstream of polyadenylation sites (5,6). SRSF3 has been shown to be regulated by an epitranscriptomic mechanism, as the m6a-binding factor YTHDC1 recruits SRSF3 to promote exon inclusion, while blocking the binding of SRSF10 (7). SRSF3 has been identified as an oncogene, which through its autoregulation and alternative splicing of other proteins, can drive many different cancer types (8-12).