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Recombinant Human U4/U6 small nuclear ribonucleoprotein Prp3 (PRPF3)

ACP20958

Number
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High Purity LevelsPrecision and ReliabilityCustomization Options

Specifications


Cat.No ACP20958 Target NamePRPF3
FormLyophilized powderExpression SystemCustom Production. Please inquire and provide the desire expression system.
Expression Range1-683Protein LengthFull length protein
Purity>85% (SDS-PAGE)Storage Buffer5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0.

Immunogen Information


Target SpeciesHumanUniprot IDO43395
Background Information
  • Uniprot Id

    O43395

  • Target Species

    Human

  • Target Name

    PRPF3

  • Target Full Name

    U4/U6 small nuclear ribonucleoprotein Prp3

  • Target Function

    Plays role in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex).

  • Target Involvement

    Retinitis pigmentosa 18 (RP18)

  • Target Subcellular Location

    Nucleus. Nucleus speckle.

  • Target Tissue Specificity

    Highly expressed in retina, liver, kidney and blood. Detected at lower levels in heart and brain.

  • Target Synonyms

    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

  • Target Background

    The removal of introns from nuclear pre-mRNAs occurs on complexes called spliceosomes, which are made up of 4 small nuclear ribonucleoprotein (snRNP) particles and an undefined number of transiently associated splicing factors. This gene product is one of several proteins that associate with U4 and U6 snRNPs. Mutations in this gene are associated with retinitis pigmentosa-18.

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