epitope mapping at the C-terminus of FBP21 of human origin
recommended for detection of FBP21 of mouse, rat and human origin by WB, IF and ELISA; also reactive with additional species, including equine, canine and bovine
FBP21 Background Information WW domains mediate protein-protein interactions through binding to short proline-rich motifs within their respective ligands. The WW domain is composed of approximately 40 amino acids that fold as a stable, triple stranded beta-sheet without disulfide bridges or cofactors. Proteins containing the WW domain are found in a wide range of signaling proteins, which can be localized within the cytoplasm or the nucleus. FBP21, also known as WW domain-binding protein 4, is a 376 amino acid protein that contains two WW domains and is characterized as a spliceosome-associated protein. FBP21 localizes to nucleus speckles and is thought to play a role in cross-intron bridging of U1 and U2 snRNPs in the mammalian A complex. Specifically, FBP21 interacts via its WW domains with the proline-rich domain of Sam 68 and also binds splicing factors Sm B/B', hnRNP C1/C2 and splicing factor 1.
