Amylins (IAPP) and Fragments

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.

References

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.