Islet amyloid polypeptide (IAPP, amylin), is a 37-residue peptide hormone co-secreted with insulin from the pancreatic β-cells. IAPP is processed from an 89-amino acid precursor pro-islet amyloid polypeptide (proIAPP) in pancreatic β-cells. ProIAAP undergoes complex posttranslational modifications including protease cleavage, C-terminal amidation and formation of an intramolecular disulfide bridge to produce the mature IAPP. Amyloid deposits deriving from IAPP are commonly found in pancreatic islets of patients suffering of T2DM or containing an insulinoma cancer. The human IAPP (20- 29) region that has been found to be essential to amyloid formation is thought to be a key factor in the initiation of amyloid aggregation.
Immunogen
synthetic peptide corresponding to an internal sequence of human pro-IAPP
Application
Anti-Islet Amyloid Polypeptide (IAPP) (Internal) antibody produced in rabbit has been used in immunohistochemistry.
Biochem/physiol Actions
IAPP/Amylin plays a role in glycemic regulation by slowing gastric emptying and promoting satiety, prevents post-prandial spikes in blood glucose levels. Islet amyloid formation, initiated by the aggregation of IAPP, contributes to the progressive loss of islet β-cells. IAPP, like β-amyloid peptide associated with Alzheimer′s disease, can induce apoptosis in insulin producing b-cells, an effect that is relevant to the development of type 2 diabetes. IAPP has been linked to type 2 diabetes (T2DM) and the loss of islet β-cells.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
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Islet amyloid polypeptide (IAPP, or amylin) is one of the major secretory products of β-cells of the pancreatic islets of Langerhans. It is a regulatory peptide with putative function both locally in the islets, where it inhibits insulin and glucagon
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