Rabbit Recombinant Monoclonal SFPQ antibody - conjugated to Alkaline Phosphatase.
IgG
Rabbit
Alkaline Phosphatase
pH: 7.4
Preservative: 0.1% Proclin 300 Solution
Constituents: 50% Glycerol (glycerin, glycerine), 1% BSA, 0.016% Magnesium chloride, 0.001% Zinc chloride
Liquid
Monoclonal
Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application Target Binding Affinity | Reactivity Expected | Dilution info - | Notes - |
Application Antibody Labelling | Reactivity Expected | Dilution info - | Notes - |
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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 (PubMed:25765647). 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 (PubMed:25765647). 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. 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 (By similarity). Required for the assembly of nuclear speckles (PubMed:25765647). 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 (PubMed:28712728).
100 kDa DNA-pairing protein, Polypyrimidine tract-binding protein-associated-splicing factor, hPOMp100, PSF, PTB-associated-splicing factor, PSF, SFPQ
Rabbit Recombinant Monoclonal SFPQ antibody - conjugated to Alkaline Phosphatase.
100 kDa DNA-pairing protein, Polypyrimidine tract-binding protein-associated-splicing factor, hPOMp100, PSF, PTB-associated-splicing factor, PSF, SFPQ
IgG
Rabbit
Alkaline Phosphatase
pH: 7.4
Preservative: 0.1% Proclin 300 Solution
Constituents: 50% Glycerol (glycerin, glycerine), 1% BSA, 0.016% Magnesium chloride, 0.001% Zinc chloride
Liquid
Monoclonal
EPR11847
Affinity purification Protein A
Blue Ice
1-2 weeks
+4°C
-20°C
Upon delivery aliquot
Avoid freeze / thaw cycle, Store in the dark
This conjugated primary antibody is released using a quantitative quality control method that evaluates binding affinity post-conjugation and efficiency of antibody labeling.
For suitable applications and species reactivity, please refer to the unconjugated version of this clone. This conjugated antibody is eligible for the Abcam trial program.
This product is a recombinant monoclonal antibody, which offers several advantages including:
For more information, read more on recombinant antibodies.
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.
This supplementary information is collated from multiple sources and compiled automatically.
SFPQ also known as splicing factor proline and glutamine-rich (PSF) is a multifunctional protein serving in various cellular processes. The protein weighs approximately 76 kDa and is ubiquitously expressed across different tissues. It mainly localizes in the nucleus where it interacts with RNA and other proteins. SFPQ plays essential roles in RNA splicing and transcription regulation among others.
SFPQ takes part in multiple cellular processes including RNA processing gene expression regulation and DNA repair. SFPQ forms complexes with other proteins such as NONO which enhances its ability in transcriptional control and RNA splicing. By binding to DNA and RNA SFPQ acts as a bridge that connects various molecular events important for cell function and survival.
The protein is actively involved in the modulation of RNA metabolic pathways and signal transduction. In particular SFPQ participates in the regulation of alternative splicing processes which can influence the diversity of the proteome. Functionally related proteins like FUS show interactions with SFPQ within these pathways jointly affecting gene expression dynamics.
Aberrations in SFPQ expression or function associate with neurodegenerative diseases and cancers. Mislocalization of SFPQ and its altered expression have been observed in conditions like amyotrophic lateral sclerosis (ALS) and certain leukemia types. In these disorders proteins like TDP-43 have shown associations with SFPQ contributing to the pathology through disrupted RNA processing and cellular stress responses.
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This species and application combination has not been tested, but we predict it will work based on strong homology. However, this combination is not covered by our product promise.
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