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 N-terminal glycine rich domain, a proline/glutamine-rich domain (P/Q), two RNA recognition motifs (RRMs) and a C-terminal region with two nuclear localization signals. The SFPQ gene is mapped to human chromosome 1p34.
Immunogen
SFPQ (NP_005057, 269 a.a. ~ 361 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.
Monoclonal Anti-SFPQ antibody produced in mouse has been used in Western Blotting and immunofluorescence.
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).
Physical form
Solution in phosphate buffered saline, pH 7.4
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Nature chemical biology, 19(7), 825-836 (2023-03-03)
Much of the human proteome is involved in mRNA homeostasis, but most RNA-binding proteins lack chemical probes. Here we identify electrophilic small molecules that rapidly and stereoselectively decrease the expression of transcripts encoding the androgen receptor and its splice variants
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