Analytical Data
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Gene name
IAPP
- Application
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Alternative Names
PYY-I
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Species
Human
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Source
Yeast
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P10997
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Expression Region
34-70aa
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Molecular Weight
5.9 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
The IAPP (Islet Amyloid Polypeptide), also known as amylin, is a peptide hormone co-secreted with insulin from the pancreatic beta cells. In humans, IAPP plays a crucial role in glucose metabolism and is involved in regulating appetite and gastric emptying. However, under pathological conditions, such as in type 2 diabetes, IAPP tends to misfold and aggregate, leading to the formation of amyloid plaques in the pancreas, which can contribute to beta cell dysfunction and insulin resistance. The study of IAPP and its amyloidogenic properties has garnered significant attention due to its implications in diabetes and metabolic disorders. Researchers focus on understanding the mechanisms underlying IAPP aggregation and toxicity, as well as exploring potential therapeutic strategies, including the development of inhibitors that prevent IAPP aggregation or promote its proper folding. Moreover, the exploration of IAPP’s structure-function relationship is essential for designing effective drugs aimed at mitigating its pathological effects. The reconstitution of IAPP proteins in vitro allows for detailed examination of their biophysical properties and interactions, paving the way for innovative therapeutic approaches to combat diabetes and improve metabolic health. Overall, the multifaceted role of IAPP in both physiology and pathology highlights the importance of ongoing research aimed at unraveling its complexities and potential as a target for treatment.
