SFPQ Antikörper (AA 572-622)

Produktnummer ABIN8124909

Der Kaninchen Polyklonal anti-SFPQ Antikörper wird verwendet zum Nachweis von SFPQ in Proben von Human, Maus und Ratte. Er wurde validiert für WB und ELISA.

Kurzübersicht für SFPQ Antikörper (AA 572-622) (ABIN8124909)

Target: SFPQ (Splicing Factor Proline/glutamine-Ric (SFPQ))

Reaktivität: Human, Maus, Ratte

Wirt: Kaninchen

Klonalität: Polyklonal

Konjugat: Dieser SFPQ Antikörper ist unkonjugiert

Applikation: Western Blotting (WB), ELISA

Produktdetails anti-SFPQ Antikörper

Bindungsspezifität: AA 572-622

Verwendungszweck: SFPQ Antibody

Spezifität: SFPQ Polyclonal Antibody detects endogenous levels of protein.

Aufreinigung: The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.

Immunogen: Synthesized peptide derived from part region of human protein AA range: 572-622

Isotyp: IgG

Anwendungsinformationen

Applikationshinweise: WB 1:500-2000 ELISA 1:5000-20000

Beschränkungen: Nur für Forschungszwecke einsetzbar

Handhabung

Format: Liquid

Buffer: Liquid in PBS containing 50 % glycerol, and 0.02 % sodium azide.

Konservierungsmittel: Sodium azide

Vorsichtsmaßnahmen: This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

Lagerung: -20 °C

Informationen zur Lagerung: Store at -20°C/1 year

Haltbarkeit: 12 months

Details zu SFPQ

Target: SFPQ (Splicing Factor Proline/glutamine-Ric (SFPQ))

Andere Bezeichnung: SFPQ

Hintergrund:

Background: alternative products:Additional isoforms seem to exist,caution:Was originally (PubMed:2480877) thought to be myoblast cell surface antigen 24.1D5 and a possible membrane-bound protein ectokinase.,disease:A chromosomal aberration involving SFPQ may be a cause of papillary renal cell carcinoma (PRCC). Translocation t(X,1)(p11.2,p34) with TFE3.,function: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 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.,PTM:Arg-7, Arg-9, Arg-19 and Arg-25 are dimethylated, probably to asymmetric dimethylarginine.,PTM: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.,PTM:The N-terminus is blocked.,similarity:Contains 2 RRM (RNA recognition motif) domains.,subcellular location:Predominantly in nuclear matrix.,subunit:Interacts with PSPC1 (By similarity). Monomer and component of the SFPQ-NONO complex, which is probably a heterotetramer of two 52 kDa (NONO) and two 100 kDa (SFPQ) subunits. SFPQ is a component of spliceosome and U5.4/6 snRNP complexes. Interacts with SNRPA/U1A. Component of a snRNP-free complex with SNRPA/U1A. Part of complex consisting of SFPQ, NONO and MATR3. Interacts with polypyrimidine tract-binding protein 1/PTB. Part of a complex consisting of SFPQ, NONO and NR5A1/SF-1. Interacts with RXRA, probably THRA, and SIN3A. Interacts with TOP1. Part of a complex consisting of SFPQ, NONO and TOP1. Interacts with SNRNP70 in apoptotic cells (By similarity). Interacts with RNF43.,

Gene Name: SFPQ PSF

Protein Name: Splicing factor, proline- and glutamine-rich (100 kDa DNA-pairing protein) (hPOMp100) (DNA-binding p52/p100 complex, 100 kDa subunit) (Polypyrimidine tract-binding protein-associated-splicing factor) (PSF) (PTB-associated-splicing factor)

Gen-ID: 6421

UniProt: P23246