SFPQ Protein (AA 1-699) (Strep Tag)

Produktnummer ABIN3136766

Produktdetails

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

Protein-Typ: Recombinant

Proteineigenschaft: AA 1-699

Spezies: Maus

Quelle: Tobacco (Nicotiana tabacum)

Aufreinigungstag / Konjugat: Dieses SFPQ Protein ist gelabelt mit Strep Tag.

Applikation: ELISA, Western Blotting (WB), SDS-PAGE (SDS)

Sequenz: MSRDRFRSRG GGGGGFHRRG GGGGRGGLHD FRSPPPGMGL NQNRGPMGPG PGGPKPPLPP PPPHQQQQQP PPQQPPPQQP PPHQQPPPHQ PPHQQPPPPP QESKPVVPQG PGSAPGVSSA PPPAVSAPPA NPPTTGAPPG PGPTPTPPPA VPSTAPGPPP PSTPSSGVST TPPQTGGPPP PPAGGAGPGP KPGPGPGGPK GGKMPGGPKP GGGPGMGAPG GHPKPPHRGG GEPRGGRQHH APYHQQHHQG PPPGGPGPRT EEKISDSEGF KANLSLLRRP GEKTYTQRCR LFVGNLPADI TEDEFKRLFA KYGEPGEVFI NKGKGFGFIK LESRALAEIA KAELDDTPMR GRQLRVRFAT HAAALSVRNL SPYVSNELLE EAFSQFGPIE RAVVIVDDRG RSTGKGIVEF ASKPAARKAF ERCSEGVFLL TTTPRPVIVE PLEQLDDEDG LPEKLAQKNP MYQKERETPP RFAQHGTFEY EYSQRWKSLD EMEKQQREQV EKNMKDAKDK LESEMEDAYH EHQANLLRQD LMRRQEELRR MEELHSQEMQ KRKEMQLRQE EERRRREEEM MIRQREMEEQ MRRQREESYS RMGYMDPRER DMRMGGGGTM NMGDPYGSGG QKFPPLGGGG GIGYEANPGV PPATMSGSMM GSDMRTERFG QGGAGPVGGQ GPRGMGPGTP AGYGRGREEY EGPNKKPRF
Sequence without tag. The proposed Strep-Tag is based on experience s with the expression system, a different complexity of the protein could make another tag necessary. In case you have a special request, please contact us.

Produktmerkmale: Key Benefits:

• Made in Germany - from design to production - by highly experienced protein experts.
• Protein expressed with ALiCE® and purified by multi-step, protein-specific process to ensure correct folding and modification.
• These proteins are normally active (enzymatically functional) as our customers have reported (not tested by us and not guaranteed).
• State-of-the-art algorithm used for plasmid design (Gene synthesis).

This protein is a made-to-order protein and will be made for the first time for your order. Our experts in the lab will ensure that you receive a correctly folded protein.

The big advantage of ordering our made-to-order proteins in comparison to ordering custom made proteins from other companies is that there is no financial obligation in case the protein cannot be expressed or purified.

Expression System:

• ALiCE®, our Almost Living Cell-Free Expression System is based on a lysate obtained from Nicotiana tabacum c.v.. This contains all the protein expression machinery needed to produce even the most difficult-to-express proteins, including those that require post-translational modifications.
• During lysate production, the cell wall and other cellular components that are not required for protein production are removed, leaving only the protein production machinery and the mitochondria to drive the reaction. During our lysate completion steps, the additional components needed for protein production (amino acids, cofactors, etc.) are added to produce something that functions like a cell, but without the constraints of a living system - all that's needed is the DNA that codes for the desired protein!

Concentration:

• The concentration of our recombinant proteins is measured using the absorbance at 280nm.
• The protein's absorbance will be measured in several dilutions and is measured against its specific reference buffer.
• We use the Expasy's protparam tool to determine the absorption coefficient of each protein.

Aufreinigung: Two step purification of proteins expressed in Almost Living Cell-Free Expression System (ALiCE®):

1. In a first purification step, the protein is purified from the cleared cell lysate using StrepTag capture material. Eluate fractions are analyzed by SDS-PAGE.
2. Protein containing fractions of the best purification are subjected to second purification step through size exclusion chromatography. Eluate fractions are analyzed by SDS-PAGE and Western blot.

Reinheit: ≥ 80 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.

Endotoxin-Niveau: Low Endotoxin less than 1 EU/mg (< 0.1 ng/mg)

Güteklasse: Crystallography grade

Anwendungsinformationen

Applikationshinweise: In addition to the applications listed above we expect the protein to work for functional studies as well. As the protein has not been tested for functional studies yet we cannot offer a guarantee though.

Kommentare:

ALiCE®, our Almost Living Cell-Free Expression System is based on a lysate obtained from Nicotiana tabacum c.v.. This contains all the protein expression machinery needed to produce even the most difficult-to-express proteins, including those that require post-translational modifications.
During lysate production, the cell wall and other cellular components that are not required for protein production are removed, leaving only the protein production machinery and the mitochondria to drive the reaction. During our lysate completion steps, the additional components needed for protein production (amino acids, cofactors, etc.) are added to produce something that functions like a cell, but without the constraints of a living system - all that's needed is the DNA that codes for the desired protein!

Beschränkungen: Nur für Forschungszwecke einsetzbar

Handhabung

Format: Liquid

Buffer: The buffer composition is at the discretion of the manufacturer. If you have a special request, please contact us.

Handhabung: Avoid repeated freeze-thaw cycles.

Lagerung: -80 °C

Informationen zur Lagerung: Store at -80°C.

Haltbarkeit: Unlimited (if stored properly)

Antigendetails

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

Andere Bezeichnung: Sfpq (SFPQ Produkte)

Synonyme: 1110004P21Rik Protein, 2810416M14Rik Protein, 5730453G22Rik Protein, 9030402K04Rik Protein, AU021830 Protein, D4Ertd314e Protein, Gm12940 Protein, OTTMUSG00000009329 Protein, PSF Protein, REP1 Protein, hm:zeh0027 Protein, wu:fa11h12 Protein, wu:fd10f03 Protein, zgc:85935 Protein, POMP100 Protein, splicing factor proline/glutamine rich (polypyrimidine tract binding protein associated) Protein, splicing factor proline/glutamine-rich Protein, splicing factor proline and glutamine rich Protein, Sfpq Protein, sfpq Protein, SFPQ Protein

Hintergrund: Splicing factor, proline- and glutamine-rich (DNA-binding p52/p100 complex, 100 kDa subunit) (Polypyrimidine tract-binding protein-associated-splicing factor) (PSF) (PTB-associated-splicing factor),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 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. 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 a transcriptional activator (By similarity). 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 a 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 (By similarity). Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex through histone deacetylation (PubMed:21680841, PubMed:22966205). Required for the assembly of nuclear speckles (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:P23246, ECO:0000269|PubMed:21680841, ECO:0000269|PubMed:22966205}.

Molekulargewicht: 75.4 kDa

UniProt: Q8VIJ6