Technical Data

133223-HRP
Clone Type
Monoclonal
Host
Mouse
Source
Human
Conjugate
HRP
Isotype
IgG2a,k
Clone Number
6D7
Grade
Affinity Purified
Applications
E IHC WB
Crossreactivity
Hu
Accession #
NM_005066, NP_005057
Shipping Temp
Blue Ice
Storage Temp
-20°C
Notes
Preservative Free
BSA Free
Mouse Anti-SFPQ (Splicing Factor, Proline- and Glutamine-rich, 100kD DNA-pairing Protein, hPOMp100, DNA-binding p52/p100 Complex, 100kD Subunit, Polypyrimidine Tract-binding Protein-associated-splicing Factor, PSF, PTB-associated-splicing Fact, PSF) (HRP)

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.

Applications
Suitable for use in ELISA, Western Blot, Immunohistochemistry. Other applications not tested.
Recommended Dilution
Immunohistochemistry (Formalin fixed paraffin embedded): 3ug/ml Optimal dilutions to be determined by the researcher.
AA Sequence
EEKISDSEGFKANLSLLRRPGEKTYTQRCRLFVGNLPADITEDEFKRLFAKYGEPGEVFINKGKGFGFIKLESRALAEIAKAELDDTPMRGRQ*
Storage and Stability
Store product at 4°C if to be used immediately within two weeks. For long-term storage, aliquot to avoid repeated freezing and thawing and store at -20°C. Aliquots are stable at -20°C for 12 months after receipt. Dilute required amount only prior to immediate use. Further dilutions can be made in assay buffer. Note: Sodium azide is a potent inhibitor of peroxidase and should not be added to HRP conjugates. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Note: Applications are based on unconjugated antibody.
Immunogen
Partial recombinant corresponding to aa269-362 from human SFPQ (NP_005057) with GST tag. MW of the GST tag alone is 26kD.
Form
Supplied as a liquid in PBS, pH 7.2. No preservative added. Labeled with horseradish peroxidase (HRP).
Purity
Purified by Protein A affinity chromatography.
Specificity
Recognizes human SFPQ.

Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.

References
1. Novel snail1 target proteins in human colon cancer identified by proteomic analysis. Larriba MJ, Casado-Vela J, Pendas-Franco N, Pena R, Garcia de Herreros A, Berciano MT, Lafarga M, Casal JI, Munoz A.PLoS One. 2010 Apr 20;5(4):e10221, 2. A cell-based screen for splicing regulators identifies hnRNP LL as a distinct signal-induced repressor of CD45 variable exon 4. Topp JD, Jackson J, Melton AA, Lynch KW.RNA. 2008 Oct;14(10):2038-49. Epub 2008 Aug 21, 3. Combinatorial Control of Signal-Induced Exon Repression by HnRNP L and PSF. Melton AA, Jackson J, Wang J, Lynch KW.Mol Cell Biol. 2007 Oct;27(19):6972-84. Epub 2007 Jul 30.
USBio References
No references available
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