Analytical Data
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Gene name
GIPR
- Application
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Alternative Names
GIPR；Gastric inhibitory polypeptide receptor
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P48546
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Expression Region
22-138aa
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AA Sequence
RAETGSKGQTAGELYQRWERYRRECQETLAAAEPPSGLACNGSFDMYVCW DYAAPNATARASCPWYLPWHHHVAAGFVLRQCGSDGQWGLWRDHTQCENP EKNEAFLDQRLILERLQ
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Molecular Weight
19 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
Related Products
Protein Description
GIPR (Gastric Inhibitory Polypeptide Receptor) is a crucial member of the glucagon-like peptide receptor family, primarily involved in regulating glucose homeostasis and insulin secretion. Its role in adipogenesis and metabolism makes it a target of considerable interest in diabetes and obesity research. Recent studies have indicated that GIPR is expressed in various tissues, including pancreatic beta cells, adipose tissue, and the brain, suggesting it may play diverse physiological roles beyond its initial identification in the gastrointestinal system. The challenge in studying GIPR has been the difficulty in obtaining sufficient quantities of functional recombinant protein, which is essential for detailed molecular characterization and high-throughput screening of potential therapeutics. Advances in recombinant DNA technology and protein expression systems have opened new avenues for producing GIPR proteins, allowing researchers to investigate their structure, function, and interactions with ligands. This research is particularly relevant in the context of developing novel treatments for metabolic disorders, as understanding the detailed mechanisms of GIPR activity could lead to more effective strategies for managing insulin resistance and promoting metabolic health. Ultimately, the study of GIPR and the production of its recombinant protein offers significant promise for uncovering new insights into endocrine regulation and potential therapeutic interventions.
