Cat: IPD-X39893

Recombinant Escherichia coli manA Protein ,His & SUMO

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Analytical Data

  • Gene name

    manA

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    PhosphohexomutasePhosphomannose isomerase ;PMI

  • Species

    Escherichia coli

  • Source

    E. coli

  • Tag

    N- His-SUMO

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P00946

  • Expression Region

    1-391aa

  • Molecular Weight

    58.8 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

ManA, or mannose-6-phosphate isomerase, is an important enzyme that plays a crucial role in the mannose-6-phosphate (M6P) pathway, which is vital for protein glycosylation and cellular signaling. Research on ManA recombinant proteins has gained significant attention due to their potential applications in biomedical fields, including drug development and gene therapy. The M6P pathway is essential for the proper trafficking of lysosomal enzymes and for the regulation of various cellular processes, including receptor-mediated endocytosis. Abnormalities in this pathway are linked to several diseases, including lysosomal storage disorders and cancer, making ManA an attractive target for therapeutic interventions. The study of ManA recombinant proteins involves their expression, purification, and characterization, aiming to understand their structure-function relationship and develop potential enzyme replacement therapies. Advances in molecular cloning and expression technologies have enabled researchers to produce high-yield recombinant ManA proteins, facilitating detailed biochemical studies and the exploration of their pharmacological potential. Understanding the functional dynamics of ManA not only enhances our knowledge of cellular metabolism but also opens pathways for innovative therapeutic strategies in managing diseases associated with glycosylation defects. This is particularly important for developing novel treatments that leverage the enzyme's specificity and mechanism, potentially leading to improved outcomes for patients with related metabolic disorders. Overall, ongoing research into ManA recombinant proteins holds promise for fostering advancements in therapeutic applications and understanding fundamental biological processes.

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