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.

SFPQ (NP_005057, 269 a.a. ~ 361 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.

Sequence
EEKISDSEGFKANLSLLRRPGEKTYTQRCRLFVGNLPADITEDEFKRLFAKYGEPGEVFINKGKGFGFIKLESRALAEIAKAELDDTPMRGRQ

Monoclonal Anti-SFPQ antibody produced in mouse has been used in Western Blotting and immunofluorescence.

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).

Solution in phosphate buffered saline, pH 7.4

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