Amylins (IAPP) and Fragments

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CAT# Product Name M.W Molecular Formula Inquiry
A12001 Amylin(20-29), Islet Amyloid Polypeptide, IAPP (20-29), rat 1007.2 Inquiry
A12002 Amylin (20-29), human 1009.1 Inquiry
A12003 Amylin(20-29), Islet Amyloid Polypeptide, IAPP (20-29), cat 1019.1 Inquiry
A12004 Amylin(20-29), Islet Amyloid Polypeptide, IAPP (20-29), hamster 1024.2 Inquiry
A12006 Amylin (1-13), human 1378.6 Inquiry
A12009 Amylin (8-37), human 3183.5 Inquiry
A12011 Acetyl-Amylin (8-37) (human) 3225.53 C140H218N42O46 Inquiry
A12012 Acetyl-Amylin (8-37), rat 3243.7 Inquiry
A12013 Amylin (1-37), human, amide 3903.3 Inquiry
A12014 Amylin, human, free acid 3904.3 C165H258N50O55S2 Inquiry
A12015 Amylin (1-37), human 3906.3 Inquiry
A12016 Amylin, rat 3920.5 C167H272N52O53S2 Inquiry
A12017 Pramlintide, Acetate [Pro25, 28, 29]-Amylin(1-37) (human), Amide 3949.6 C171H269N51O53S2 Inquiry
A12018 5-FAM-Amylin (mouse, rat) 4278.75 C188H282N52O59S2 Inquiry
A12019 Amylin (14-20) (human) 802.89 C36H54N10O11 Inquiry
A12020 Amylin (20-29) (human) 1009.1 C43H68N12O16 Inquiry
CAD-108 Biotinyl-Amylin (human) 4129.63 C₁₇₅H₂₇₅N₅₃O₅₇S₃ Inquiry
CAD-109 5-FAM-Amylin (human) 4261.64 C₁₈₆H₂₇₁N₅₁O₆₁S₂ Inquiry
R1187 Amylin (8-37), rat 3200.61 C₁₄₀H₂₂₇N₄₃O₄₃ Inquiry

Amylin, also known as islet amyloid-like polypeptide (IAPP), is a polypeptide composed of 37 amino acid residues, stimulated by glucose or other nutrients, secreted by islet β cells and insulin at the same time. Studies have shown that the amino acid sequence of human amylin 20-29 is the sequence of amyloid production, which can produce amyloid accumulation in pancreatic islets, have toxic effects on β cells, and have been insulin secretion. Leading to insulin secretion disorder and β cell failure may play an important role in the secondary failure of sulfonylurea drugs and β cell failure in type 2 diabetes mellitus.

The role of amylin in the physiology of glycemic control

Amylin is co-located and secreted with insulin under the action of nutritional stimulation. Like insulin, amylin deficiency was found in patients with type 1 diabetes, while changes in plasma starch levels in patients with impaired glucose tolerance and type 2 diabetes were similar to those in insulin. It has been well confirmed that insulin regulates blood glucose control by promoting glucose release. Some research have showed the evidence in animals and diabetic patients that amylin regulates glucose inflow circulation by delaying the release of nutrients, so as to inhibiting the appearance of postprandial glucose and inhibiting the secretion of glucagon after meal. Therefore, we believe that the role of amylin is a supplement to insulin. Despite insulin replacement therapy, the problem of blood glucose control in diabetic patients may be due to amylin deficiency.

Function of Amylins (IAPP)

  • Amylin is part of the endocrine pancreas and helps control blood sugar. The peptide is secreted from the islets into the blood circulation and removed by peptidase in the kidney.
  • The metabolic function of amylin is to inhibit the appearance of nutrition in plasma. Therefore, it is a synergistic partner of insulin, which binds to islet β cells together with insulin as a dietary response. The overall effect is to slow down the rate of glucose in the blood after eating (Ra), which is achieved by coordinating the reduction of gastric emptying and inhibition of digestive secretion, therefore reducing food intake.
  • Amylin is also involved in bone metabolism with calcitonin and calcitonin gene-related peptide.
  • Amylin gene knockout in rodents does not normally reduce appetite after eating. Because it is an amide peptide, like many neuropeptides, it is thought to be the cause of appetite.


  1. Goldsbury, C., Goldie, K., Pellaud, J., Seelig, J., Frey, P., Müller, S. A., ... & Aebi, U. (2000). Amyloid fibril formation from full-length and fragments of amylin. Journal of structural biology, 130(2-3), 352-362.
  2. Kanatsuka, A., Kou, S., & Makino, H. (2018). IAPP/amylin and β-cell failure: implication of the risk factors of type 2 diabetes. Diabetology international, 9(3), 143-157.
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