SFPQ, also named PSF, encodes a nuclear factor implicated in the splicing and regulation of gene expression. SFPQ probably forms a heteromer with NONO and participates in DNA pairing and DNA break repair program. Very recently SFPQ was identified as a downstream target of tau, complete nuclear depletion and cytoplasmic accumulation of SFPQ were shown in the neurons and astrocytes of brains with Alzheimer's disease (AD), more strikingly, reduced SFPQ levels may progress together with tau pathology, these observation strongly suggests the important role of SFPQ pathology in neurodegenerative diseases including AD. SFPQ protein may appears as 47 kDa, 52 kDa or 100 kDa molecules in various cell types. This antibody is a rabbit polyclonal antibody raised against the N-terminal of human SFPQ.
Categories
Primary Antibodies
Clonality
polyclonal
Description
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 alteative 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 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. 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 avtivity. 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. 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.
Host
Rabbit
Immunogen
splicing factor proline/glutamine-rich (polypyrimidine tract binding protein associated)
Isotype
IgG
Molecular Weight
115 kDa
Reactivity
Human, Mouse, Rat
Regulatory
RUO
Synonyms
PSF
Uniprot
P23246
Gene Id
6421
Research Area
Metabolism, Neuroscience
Form
liquid
Format
liquid
Purification
Immunogen affinity purified
Purity
>=95% as determined by SDS-PAGE
Storage
PBS with 0.02% sodium azide and 50% glycerol pH 7.3, -20°C for 12 months (Avoid repeated freeze / thaw cycles.)