Cat: IPD-X39090

Recombinant Human PGM5 Protein,His

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Analytical Data

  • Gene name

    PGM5

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    PGMRP; Phosphoglucomutase-Related Protein; Aciculin; Phosphoglucomutase-like protein 5

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q15124

  • Expression Region

    Leu182~Gly296

  • Molecular Weight

    19kDa

  • 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

The PGM5 (Phosphoglucomutase 5) protein, a member of the phosphoglucomutase family, plays a significant role in carbohydrate metabolism and cellular function. It is primarily involved in the interconversion of glucose-1-phosphate and glucose-6-phosphate, critical processes for energy production and glycogen metabolism. Recent studies have highlighted the importance of PGM5 not only in metabolic regulation but also in cancer biology, where altered expression levels of PGM5 have been linked to tumor progression and metastasis. Researchers are increasingly interested in PGM5 as a potential biomarker and therapeutic target due to its association with various diseases, including metabolic disorders and cancers. The investigation of recombinant PGM5 proteins allows for a deeper understanding of its structural properties, enzymatic mechanisms, and interactions with other cellular components. Additionally, the production of recombinant PGM5 enables the exploration of its functional roles in vivo and in vitro, providing crucial insights into its biological significance. This growing interest in PGM5 underscores the need for detailed characterization of its functions and pathways, paving the way for innovative therapeutic strategies that could leverage its activity in disease contexts. Overall, the study of PGM5 recombinant proteins is a promising avenue for advancing our comprehension of metabolic pathways and disease mechanisms.

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