Cat: PAX2000-10582

Recombinant Human PRPF3 Protein,His

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Analytical Data

  • Gene name

    PRPF3

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    hPrp3; HPRP3P; Pre mRNA splicing factor 3; Pre-mRNA-splicing factor 3; Precursor mRNA-processing factor 3; S. crevisiae; homolog of; PRP3 pre-mRNA processing factor 3 homolog (S. cerevisiae); Prp3p; PRPF3; PRPF3_HUMAN; RP18; SNRNP90; U4/U6 small nuclear ribonucleoprotein PRP3; U4/U6 snRNP 90 kDa protein

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    O43395

  • Expression Region

    1-683 aa

  • AA Sequence

    MALSKRELDE LKPWIEKTVK RVLGFSEPTV VTAALNCVGK GMDKKKAADH LKPFLDDSTL RFVDKLFEAV EEGRSSRHSK SSSDRSRKRE LKEVFGDDSE ISKESSGVKK RRIPRFEEVE EEPEVIPGPP SESPGMLTKL QIKQMMEAAT RQIEERKKQL SFISPPTPQP KTPSSSQPER LPIGNTIQPS QAATFMNDAI EKARKAAELQ ARIQAQLALK PGLIGNANMV GLANLHAMGI APPKVELKDQ TKPTPLILDE QGRTVDATGK EIELTHRMPT LKANIRAVKR EQFKQQLKEK PSEDMESNTF FDPRVSIAPS QRQRRTFKFH DKGKFEKIAQ RLRTKAQLEK LQAEISQAAR KTGIHTSTRL ALIAPKKELK EGDIPEIEWW DSYIIPNGFD LTEENPKRED YFGITNLVEH PAQLNPPVDN DTPVTLGVYL TKKEQKKLRR QTRREAQKEL QEKVRLGLMP PPEPKVRISN LMRVLGTEAV QDPTKVEAHV RAQMAKRQKA HEEANAARKL TAEQRKVKKI KKLKEDISQG VHISVYRVRN LSNPAKKFKI EANAGQLYLT GVVVLHKDVN VVVVEGGPKA QKKFKRLMLH RIKWDEQTSN TKGDDDEESD EEAVKKTNKC VLVWEGTAKD RSFGEMKFKQ CPTENMAREH FKKHGAEHYW DLALSESVLE STD

  • Molecular Weight

    77.5 kDa

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • 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.

  • 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.

  • 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

PRPF3 (Pre-mRNA processing factor 3) is a crucial component of the spliceosome, playing a significant role in the pre-mRNA splicing process that is essential for the maturation of mRNA. This protein is involved in the assembly of the spliceosomal complex and is necessary for the recognition of splice sites on pre-mRNA. Research has highlighted PRPF3's importance in gene expression regulation and its connection to various diseases, particularly retinitis pigmentosa, a hereditary eye disorder leading to vision loss caused by mutations in splicing factors. Understanding the structure and function of PRPF3 through studies of its recombinant protein is critical for elucidating its role in the splicing machinery. This research can potentially uncover the molecular mechanisms underlying splicing-related diseases and may pave the way for therapeutic strategies that target splicing defects. Recombinant PRPF3 can be used in biochemical assays to characterize its interactions with other spliceosomal components, study the effects of disease-associated mutations, and explore its regulatory functions in cellular contexts. As splicing is a fundamental cellular process, PRPF3's study could also contribute to broader insights into RNA processing, gene regulation, and the development of novel interventions for splicing-related disorders.

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