Analytical Data
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Gene name
IAPP
- Application
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Alternative Names
IAPP；Islet amyloid polypeptide
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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
P10997
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Expression Region
34-70aa
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AA Sequence
KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY
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Molecular Weight
31.4 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 research on IAPP (islet amyloid polypeptide) recombinant proteins has gained significant attention due to their implications in diabetes mellitus, particularly Type 2 diabetes. IAPP, co-secreted with insulin by pancreatic beta cells, plays a crucial role in glucose metabolism and appetite regulation. However, under pathological conditions, IAPP can misfold and aggregate to form amyloid fibrils, which are toxic to beta cells and contribute to beta-cell dysfunction and death. The increasing prevalence of Type 2 diabetes worldwide has prompted investigations into the mechanisms underlying IAPP aggregation and its role in disease progression. By studying recombinant forms of IAPP, researchers aim to elucidate the molecular pathways involved in amyloid formation and investigate potential therapeutic approaches to prevent or reverse beta-cell damage. Understanding the folding properties and aggregation behavior of these recombinant proteins can lead to the development of novel strategies that may include amyloid inhibitors, anti-aggregating agents, and regenerative therapies for diabetic patients. This research is not only vital for advancing our knowledge of diabetes pathology but also holds promise for innovative treatment options that could improve the quality of life for millions affected by this chronic condition.
