Cat: IPD-X50429

Recombinant Human ADPGK Protein,full length

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Analytical Data

  • Gene name

    ADPGK

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    ADP dependent glucokinase; ADP GK; ADP-dependent glucokinase

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9BRR6

  • Expression Region

    1-497aa

  • Molecular Weight

    53kDa

  • Endotoxin

    < 1.0 EU per ug 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

ADPGK (adenosine diphosphate glucose pyrophosphorylase kinase) is an enzyme involved in the regulation of carbohydrate metabolism, particularly in the synthesis and breakdown of glycogen and starch. As a member of the glucose-1-phosphate uridylyltransferase family, ADPGK plays a critical role in phosphorylating ADP-glucose, a key substrate for glycogen synthesis. Recent studies have highlighted its importance not only in energy homeostasis but also in cellular signaling pathways. Given the increasing prevalence of metabolic disorders such as diabetes and obesity, understanding ADPGK's mechanism and functionality has garnered significant interest. Researchers have focused on the structural and functional characterization of recombinant ADPGK to investigate its enzymatic activity, regulatory mechanisms, and potential interactions with other metabolic enzymes. The development of recombinant ADPGK proteins allows for detailed studies that can elucidate its role in glucose metabolism and potentially identify novel therapeutic targets for metabolic diseases. By employing techniques such as site-directed mutagenesis, enzyme kinetics, and structural biology, researchers aim to dissect the complexities of ADPGK function and improve our understanding of its contribution to cellular energy regulation. This research not only provides insights into basic metabolic processes but also holds promise for applications in biotechnology and medicine, paving the way for innovative strategies in treating metabolic conditions.

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