Analytical Data
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Gene name
GIP
- Application
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Alternative Names
Incretin hormone; Glucose Dependent Insulinotropic Peptide
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Species
Rat
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q06145
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Expression Region
Leu11~Leu124
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Protein Length
Partial
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Molecular Weight
43kDa
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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
Gastric inhibitory polypeptide (GIP) is an important incretin hormone produced by K cells in the small intestine, primarily in response to food intake. Its primary function is to enhance insulin secretion from pancreatic beta cells, thereby playing a crucial role in glucose homeostasis. Dysregulation of GIP signaling has been implicated in metabolic disorders such as obesity and type 2 diabetes, making it an attractive target for therapeutic intervention. In recent years, recombinant GIP proteins have gained attention for their potential use in developing novel treatments aimed at improving insulin sensitivity and managing blood glucose levels. Research efforts have focused on the characterization of GIP's structure, understanding its receptor interactions, and exploring its biological effects in various models. Advances in protein engineering techniques have enabled the production of GIP analogs with enhanced stability and bioactivity, which could lead to more effective therapeutic agents. This area of research holds promise not only for diabetes management but also for broader applications in metabolic health, highlighting the need for continued exploration of GIP's molecular mechanisms and therapeutic potential.
