Cat: PA2000-9746

Recombinant Human NOL12 Protein,GST

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Analytical Data

  • Gene name

    NOL12

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Nucleolar protein 12

  • Species

    Human

  • Source

    E. coli

  • Tag

    GST-tag at N-terminal

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9UGY1

  • Expression Region

    1-213  aa

  • AA Sequence

    MGRNKKKKRDGDDRRPRLVLSFDEEKRREYLTGFHKRKVERKKAAIEEIKQRLKEEQRKLREERHQEYLKMLAEREEALEEADELDRLVTAKTESVQYDHPNHTVTVTTISDLDLSGARLLGLTPPEGGAGDRSEEEASSTEKPTKALPRKSRDPLLSQRISSLTASLHAHSRKKVKRKHPRRAQDSKKPPRAPRTSKAQRRRLTGKARHSGE

  • Molecular Weight

    51.1 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

NOL12, a member of the nucleolar protein family, is increasingly recognized for its role in the regulation of ribosome biogenesis and cellular stress responses. Research has shown that NOL12 is involved in critical cellular processes such as pre-rRNA processing and ribosomal subunit assembly. The protein's dysregulation has been linked to various diseases, including cancer and neurological disorders, suggesting its potential as a biomarker for disease progression and therapeutic targets. Moreover, the functional characterization of NOL12 and its interactions with other nucleolar proteins are vital for understanding the intricate molecular mechanisms governing cellular homeostasis and stress adaptation. The development of recombinant NOL12 protein has enabled detailed structural and functional studies, which are essential to decipher its specific roles in the nucleolus and beyond. Through these investigations, scientists aim to unravel the complex pathways influenced by NOL12 and contribute to the broader field of molecular biology and disease research.

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