Cat: IPD-X28801

Recombinant Cynomolgus GIPR Protein (HEK293),Avi & His

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Analytical Data

  • Gene name

    GIPR

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Species

    Cynomolgus

  • Source

    HEK293

  • Tag

    C-8*His;Avi

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    XP_005589662

  • Expression Region

    G26-Q138

  • Protein Length

    Partial

  • Molecular Weight

    28-40 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

The GIPR (Gastric Inhibitory Polypeptide Receptor) is a key player in the regulation of glucose metabolism and insulin secretion. As a member of the G protein-coupled receptor family, GIPR mediates the actions of gastric inhibitory polypeptide, a hormone that plays an essential role in postprandial glucose homeostasis. In recent years, the study of GIPR has gained significant attention due to its potential implications in metabolic disorders, including type 2 diabetes and obesity. Research has shown that GIPR signaling can influence pancreatic beta-cell function and energy expenditure, thereby affecting glucose levels in the bloodstream. The development of GIPR recombinant proteins allows for detailed examination of receptor structure, function, and signaling pathways, providing insights into the mechanisms underlying GIP action. Additionally, understanding GIPR interactions may pave the way for novel therapeutic approaches aimed at enhancing insulin sensitivity and promoting weight loss. As metabolic diseases continue to rise globally, the exploration of GIPR's role opens new avenues for innovative treatments and better management of these conditions.

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