PSF Anticuerpo(G-7): sc-374502

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Pre-mRNA splicing is a critical step in the post-translational regulation of gene expression. The process of removing intron sequences from mRNA is a two-step enzymatic reaction that requires the action of the spliceosome, a large multicomponent ribonucleoprotein complex. The polypyrimidine tract-binding protein (PTB)-associated splicing factor (PSF) is a ubiquitously expressed protein that forms a complex with PTB, also designated hnRNP I, which is required for early spliceosome formation and is essential for catalytic step II. The PSF protein contains two RNA recognition motifs (RRMs), a proline- and glutamine-rich amino terminal domain, and two carboxy-terminal nuclear localization signals. PSF is localized to the nucleus in punctate structures called speckles, which are absent from nucleoli. The localization of PSF to speckles is dependent upon the presence of the second RRM motif. PSF also can associate with the DNA binding domains (DBDs) of thyroid hormone receptors and retinoic acid receptors, where it acts as a repressor by recruiting HDACs to the DBDs. PSF is expressed in neurons during development and may be involved in neuronal differentiation and maturation. PSF is proteolytically cleaved to produce a shorter fragment in myeloid cells.