Product nameAnti-SFPQ antibody [B92]
See all SFPQ primary antibodies
DescriptionMouse monoclonal [B92] to SFPQ
Tested applicationsSuitable for: ICC/IF, IP, RIA, ICC, IHC-Fr, WBmore details
Species reactivityReacts with: Mouse, Human
Tissue/ cell preparation (lysate of mouse bone marrow-derived stromal cell line.).
- Whole extract of cultured HeLa cells.
Storage instructionsShipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.
Storage bufferpH: 7.40
Preservative: 0.097% Sodium azide
Constituent: 0.0268% PBS
Concentration information loading...
PurityProtein A purified
Our Abpromise guarantee covers the use of ab11825 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|ICC/IF||Use at an assay dependent concentration. PubMed: 20082308|
|IP||Use at an assay dependent concentration. (see Lee et al reference, Carramolino et al reference).|
|RIA||Use at an assay dependent concentration. (see Lee et al reference).|
|AP||Use at an assay dependent concentration. (see Shav-Tal et al reference).|
|ICC||Use at an assay dependent concentration. (see Lee et al reference).|
|IHC-Fr||Use at an assay dependent concentration.|
|WB||Use a concentration of 2 - 4 µg/ml. Detects a band of approximately 47, 49, 100, 68, 120, 100, 80, 68 kDa (predicted molecular weight: 76 kDa). (See Lee et al reference, Shav-Tal et al reference).|
FunctionDNA- 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 an heteromer with NONO. Binds to pre-mRNA in spliceosome C complex, and specifically binds to intronic polypyrimidine tracts. 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 nonhomologous 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 probably mediated by an interaction of SFPQ with SIN3A and subsequent recruitment of histone deacetylases (HDACs). The SFPQ-NONO/SF-1 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.
Involvement in diseaseNote=A chromosomal aberration involving SFPQ may be a cause of papillary renal cell carcinoma (PRCC). Translocation t(X;1)(p11.2;p34) with TFE3.
Sequence similaritiesContains 2 RRM (RNA recognition motif) domains.
modificationsThe N-terminus is blocked.
Phosphorylated on multiple serine and threonine residues during apoptosis. In vitro phosphorylated by PKC. Phosphorylation stimulates binding to DNA and D-loop formation, but inhibits binding to RNA.
Arg-7, Arg-9, Arg-19 and Arg-25 are dimethylated, probably to asymmetric dimethylarginine.
Cellular localizationNucleus matrix. Predominantly in nuclear matrix.
- Information by UniProt
- 100 kDa DNA pairing protein antibody
- 100 kDa DNA-pairing protein antibody
- 100 kDa subunit antibody
This product has been referenced in:
- Luisier R et al. Intron retention and nuclear loss of SFPQ are molecular hallmarks of ALS. Nat Commun 9:2010 (2018). Read more (PubMed: 29789581) »
- Hu L et al. Hypoxia exposure upregulates MALAT-1 and regulates the transcriptional activity of PTB-associated splicing factor in A549 lung adenocarcinoma cells. Oncol Lett 16:294-300 (2018). Read more (PubMed: 29928414) »