Splicing factor proline and glutamine rich (SFPQ), also known as polypyrimidine tract-binding protein-associated-splicing factor (PSF), is a multifunctional nuclear protein. The protein is characterized with an amino-terminal glycine rich domain, a proline/glutamine-rich domain, two RNA recognition motifs (RRMs) and a carboxy-terminal region with two nuclear localization signals. The SFPQ gene is mapped to human chromosome 1p34.
Synonyms: PPP1R140; PSF
Storage: -20C
Application: All Prestige Antibodies Powered by Atlas Antibodies are developed and validated by the Human Protein Atlas (HPA) project (www.proteinatlas.org)and as a result, are supported by the most extensive characterization in the industry. The Human Protein Atlas project can be subdivided into three efforts: Human Tissue Atlas, Cancer Atlas, and Human Cell Atlas. The antibodies that have been generated in support of the Tissue and Cancer Atlas projects have been tested by immunohistochemistry against hundreds of normal and disease tissues and through the recent efforts of the Human Cell Atlas project, many have been characterized by immunofluorescence to map the human proteome not only at the tissue level but now at the subcellular level. These images and the collection of this vast data set can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit sigma.com/prestige.
Biochem Physiol Actions: Splicing factor proline and glutamine rich (SFPQ), along with its binding partner non-POU domain-containing octamer-binding protein (NONO/p54nrb), plays a vital role in RNA processing, RNA splicing and transcriptional regulation. Additionally, these proteins also play a regulatory role in selective nuclear retention of defective mRNAs. SFPQ participates in transcription repression by recruiting transcription regulator proteins Sin3a and histone deacetylase (HDAC).
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