Cat: IPD-X31022

Recombinant Human LMW-PTP/ACP1 Protein,GST

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Analytical Data

  • Gene name

    LMW-PTP/ACP1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Adipocyte acid phosphatase Low molecular weight cytosolic acid phosphatase (EC:3.1.3.2) Red cell acid phosphatase 1

  • Species

    Human

  • Source

    E. coli

  • Tag

    N- GST

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P24666

  • Expression Region

    1-158aa

  • Molecular Weight

    45 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.

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Protein Description

Ribonuclease UK114, also known as HRSP12, is a member of the ribonuclease family that has garnered attention due to its potential roles in cellular processes and its therapeutic implications. Initially isolated from the human pancreas, this enzyme is characterized by its ability to degrade RNA substrates, which highlights its significance in RNA metabolism and regulation. Research into HRSP12 has expanded, revealing its involvement in various biological functions, including apoptosis, immune response, and tumor suppression. Given its unique enzymatic properties, HRSP12 has been of particular interest in the development of novel biotherapeutics, especially in the context of highly specific RNA targeting for antiviral and anticancer applications. By utilizing recombinant DNA technology, scientists have been able to produce HRSP12 in a controlled laboratory setting, facilitating in-depth studies of its structure-function relationships and enzymatic mechanisms. This recombinant approach not only allows for the investigation of its potential as a therapeutic agent but also enhances our understanding of its biological roles, paving the way for innovative strategies in disease treatment and intervention. Through ongoing research, the promise of Ribonuclease UK114/HRSP12 continues to be explored, with implications that could extend from basic science to clinical applications.

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