Analytical Data
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Gene name
SFPQ
- Application
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Alternative Names
100 kDa DNA pairing protein; 100 kDa DNA-pairing protein; 100 kDa subunit; DNA binding p52/p100 complex 100 kDa subunit; DNA-binding p52/p100 complex; hPOMp100; Polypyrimidine tract binding protein associated splicing factor; Polypyrimidine tract-binding protein-associated-splicing factor; POMP100; PPP1R140; proline- and glutamine-rich; Protein phosphatase 1 regulatory subunit 140; PSF; PTB associated splicing factor; PTB-associated-splicing factor; Sfpq; SFPQ_HUMAN; Splicing factor; Splicing factor proline and glutamine rich; Splicing factor proline/glutamine rich (polypyrimidine tract binding protein associated); Splicing factor proline/glutamine rich
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P23246
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Expression Region
1-707 aa
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AA Sequence
MSRDRFRSRG GGGGGFHRRG GGGGRGGLHD FRSPPPGMGL NQNRGPMGPG PGQSGPKPPI PPPPPHQQQQ QPPPQQPPPQ QPPPHQPPPH PQPHQQQQPP PPPQDSSKPV VAQGPGPAPG VGSAPPASSS APPATPPTSG APPGSGPGPT PTPPPAVTSA PPGAPPPTPP SSGVPTTPPQ AGGPPPPPAA VPGPGPGPKQ GPGPGGPKGG KMPGGPKPGG GPGLSTPGGH PKPPHRGGGE PRGGRQHHPP YHQQHHQGPP PGGPGGRSEE KISDSEGFKA NLSLLRRPGE KTYTQRCRLF VGNLPADITE DEFKRLFAKY GEPGEVFINK GKGFGFIKLE SRALAEIAKA ELDDTPMRGR QLRVRFATHA AALSVRNLSP YVSNELLEEA FSQFGPIERA VVIVDDRGRS TGKGIVEFAS KPAARKAFER CSEGVFLLTT TPRPVIVEPL EQLDDEDGLP EKLAQKNPMY QKERETPPRF AQHGTFEYEY SQRWKSLDEM EKQQREQVEK NMKDAKDKLE SEMEDAYHEH QANLLRQDLM RRQEELRRME ELHNQEMQKR KEMQLRQEEE RRRREEEMMI RQREMEEQMR RQREESYSRM GYMDPRERDM RMGGGGAMNM GDPYGSGGQK FPPLGGGGGI GYEANPGVPP ATMSGSMMGS DMRTERFGQG GAGPVGGQGP RGMGPGTPAG YGRGREEYEG PNKKPRF
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Molecular Weight
76.1 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
SFPQ (Splicing Factor Proline-Glutamine Rich) is a multifunctional protein involved in various cellular processes, including pre-mRNA splicing, DNA repair, and transcription regulation. Its significance in intracellular mechanisms has drawn considerable scientific interest, particularly due to its role in tumorigenesis and neurodegenerative diseases. SFPQ interacts with numerous proteins and RNA entities, playing a crucial role in the assembly of RNA-protein complexes and the regulation of gene expression. Abnormalities in SFPQ function and localization have been implicated in several pathologies, notably in cancers where its expression levels are often dysregulated, leading to disrupted splicing and altered cellular functions. Furthermore, recent research has suggested that SFPQ may be involved in the neurosensitive response to stress, linking it to conditions like Alzheimer's disease. Given its pivotal role in maintaining cellular homeostasis and intricate involvement in disease mechanisms, understanding SFPQ's structural features and functional dynamics through studies on its recombinant forms becomes essential for exploring targeted therapeutic strategies. The research surrounding SFPQ recombinant protein focuses on elucidating its interactions, post-translational modifications, and functional domains, which can reveal insights into its roles in health and disease. This knowledge not only contributes to the basic understanding of RNA biology but also opens avenues for the development of innovative treatments for disorders associated with SFPQ dysregulation.
