Sfpq (NM_023603) Mouse Recombinant Protein
CAT#: TP510120
Purified recombinant protein of Mouse splicing factor proline/glutamine rich (polypyrimidine tract binding protein associated) (Sfpq), with C-terminal MYC/DDK tag, expressed in HEK293T cells, 20ug
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Specifications
Product Data | |
Species | Mouse |
Expression Host | HEK293T |
Expression cDNA Clone or AA Sequence |
A DNA sequence from Mouse cDNA ORF Clone, MR210120, encoding Mouse full-length Sfpq.
|
Tag | C-MYC/DDK |
Predicted MW | 75.9 kDa |
Concentration | >0.05 µg/µL as determined by microplate BCA method |
Purity | > 80% as determined by SDS-PAGE and Coomassie blue staining |
Buffer | 25 mM Tris-HCl, 100 mM glycine, pH 7.3, 10% glycerol |
Note | For testing in cell culture applications, please filter before use. Note that you may experience some loss of protein during the filtration process. |
Storage | Store at -80°C after receiving vials. |
Stability | Stable for 12 months from the date of receipt of the product under proper storage and handling conditions. Avoid repeated freeze-thaw cycles. |
Reference Data | |
RefSeq | NP_076092 |
Locus ID | 71514 |
UniProt ID | Q8VIJ6 |
Refseq Size | 3500 |
Cytogenetics | 4 61.2 cM |
Refseq ORF | 2097 |
Synonyms | 1110004P21Rik; 2810416M14Rik; 5730453G22Rik; 9030402K04Rik; AU021830; D4Ertd314e |
Summary | DNA- and RNA binding protein, involved in several nuclear processes. Essential pre-mRNA splicing factor required early in spliceosome formation and for splicing catalytic step II, probably as a heteromer with NONO. Binds to pre-mRNA in spliceosome C complex, and specifically binds to intronic polypyrimidine tracts. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45, a phosphorylated form is sequestered by THRAP3 from the pre-mRNA in resting T-cells; T-cell activation and subsequent reduced phosphorylation is proposed to lead to release from THRAP3 allowing binding to pre-mRNA splicing regulatotry elements which represses exon inclusion. Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b. May be involved in a pre-mRNA coupled splicing and polyadenylation process as component of a snRNP-free complex with SNRPA/U1A. The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs. SFPQ may be involved in homologous DNA pairing; in vitro, promotes the invasion of ssDNA between a duplex DNA and produces a D-loop formation. The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1; in vitro, stimulates dissociation of TOP1 from DNA after cleavage and enhances its jumping between separate DNA helices. The SFPQ-NONO heteromer binds DNA. The SFPQ-NONO heteromer may be involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination and may stabilize paired DNA ends; in vitro, the complex strongly stimulates DNA end joining, binds directly to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation complex. SFPQ is involved in transcriptional regulation. Functions as transcriptional activator (By similarity). Transcriptional repression is mediated by an interaction of SFPQ with SIN3A and subsequent recruitment of histone deacetylases (HDACs). The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional activity. SFPQ isoform Long binds to the DNA binding domains (DBD) of nuclear hormone receptors, like RXRA and probably THRA, and acts as transcriptional corepressor in absence of hormone ligands. Binds the DNA sequence 5'-CTGAGTC-3' in the insulin-like growth factor response element (IGFRE) and inhibits IGF-I-stimulated transcriptional activity (By similarity). Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex through histone deacetylation (PubMed:21680841, PubMed:22966205). Required for the assembly of nuclear speckles (By similarity). Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (By similarity).[UniProtKB/Swiss-Prot Function] |
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