Cat: PA1000-8244

Recombinant Human POMP Protein,His

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Analytical Data

  • Gene name

    POMP

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    POMP;C13orf12;UMP1;Proteasome maturation Protein

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9Y244

  • Expression Region

    1-141aa

  • AA Sequence

    MNARGLGSEL KDSIPVTELS ASGPFESHDL LRKGFSCVKN ELLPSHPLEL SEKNFQLNQD KMNFSTLRNI QGLFAPLKLQ MEFKAVQQVQ RLPFLSSSNL SLDVLRGNDE TIGFEDILND PSQSEVMGEP HLMVEYKLGL L

  • 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

POMP, or proteasome maturation protein, plays a crucial role in the assembly and functionality of the 26S proteasome, which is essential for degrading damaged proteins and regulating various cellular processes, including the cell cycle and apoptosis. Research into POMP has garnered attention due to its involvement in the proteasome's biogenesis and its potential implications in diseases such as cancer and neurodegenerative disorders, where proteasome activity is often compromised. Understanding POMP’s function and the mechanisms by which it facilitates proteasome assembly can provide insights into therapeutic strategies aimed at restoring proteasome activity. Studies have shown that POMP interacts with various proteins throughout the maturation process of the proteasome, underscoring its significance in cellular homeostasis. Moreover, alterations in POMP expression levels have been linked to tumor progression, making it a potential biomarker for cancer diagnosis and treatment. Recent advancements in biotechnological methods, including cryo-electron microscopy and advanced mass spectrometry, have enabled researchers to explore the structural dynamics of POMP and its associated complexes in unprecedented detail. This growing body of research highlights the importance of POMP not only in basic cellular biology but also in the development of novel therapeutic approaches targeting proteasome dysfunctions across various diseases.

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