Cat: PA1000-1255

Recombinant E.coli glpE Protein,His

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Analytical Data

  • Gene name

    glpE

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    glpE;GPE;Glycophorin-E

  • Species

    E.coli

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    B1IP41

  • Expression Region

    1-108aa

  • AA Sequence

    MDQFECINVADAHQKLQEKEAVLVDIRDPQSFAMGHAVQAFHLTNDTLGAFMRDNDFDTPVMVMCYHGNSSKGAAQYLLQQGYDVVYSIDGGFEVWQRQFPAEVAYGA

  • Molecular Weight

    14.1 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.

Quality inspection process

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Protein Description

GLP (Glycerol-3-phosphate phosphatase-like protein E) is a member of the phosphatase family, which plays a crucial role in various metabolic processes, particularly in the regulation of glycerol-3-phosphate levels. The study of GLP is significant due to its involvement in metabolic disorders, such as obesity and diabetes, where glycerol-3-phosphate metabolism is altered. Researchers are increasingly interested in the biochemical properties and functional mechanisms of GLP-E, which could lead to potential therapeutic targets for these conditions. The expression and purification of recombinant GLP-E proteins allow for detailed structural and functional studies, enabling insights into its enzymatic activity and regulatory roles. Additionally, understanding the interaction of GLP-E with other cellular proteins could uncover novel pathways involved in energy homeostasis. As the demand for effective treatments for metabolic diseases rises, the exploration of GLP-E and its reconstitution in model systems may provide valuable information for drug development and metabolic engineering. Overall, the research on recombinant GLP-E not only advances our knowledge of glycerol metabolism but also holds promise for innovative solutions in managing metabolic syndromes.

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