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Amylin
Cat. No. CG-040
Structure:
H-Lys-Cys*-Asn-Thr-Ala-Thr-Cys*-Ala-Thr-Gln-Arg-Leu-Ala-Asn-Phe-Leu-Val-His-Ser-Ser-Asn-Asn-Phe-Gly-Ala-Ile-Leu-Ser-Ser-Thr-Asn-Val-Gly-Ser-Asn-Thr-Tyr-NH2 (disulfide bridge between cysteines 2 and 7)
Other Names:
Islet amyloid polypeptide, IAPP
Activity:
Endogenous amylin receptor agonist
Amylin (also known as islet amyloid polypeptide, or IAPP) is a centrally acting, neuroendocrine hormone and member of the calcitonin family of peptides, synthesized and cosecreted with insulin in the beta cells of pancreatic islets. Amylin inhibits glucagon secretion, delays gastric emptying and acts as a satiety agent. Amylin is a major component of the islet amyloid deposited in the pancreas in type 2 diabetes mellitus and may contribute to beta-cell degeneration.
Castillo et al (1995) Amylin/islet polypeptide: biochemistry, physiology, patho-physiology. Diabete Metab. 21 3 PMID: 7781840
Schmitz et al (2004) Amylin agonists: a novel approach in the treatment of diabetes. Diabetes. 53 Suppl 3:S233 PMID: 15561917
Bower and Hay (2016) Amylin structure-function relationships and receptor pharmacology: implications for amylin mimetic drug development. Br J Pharmacol. 173(12)1883 PMID: 27061187
Related areas
All peptides >
All calcitonin and related receptor modulators >
All endocrinology research areas >
All appetite regulation research categories >
All diabetes research categories >
Technical Data
| Structure | H-Lys-Cys*-Asn-Thr-Ala-Thr-Cys*-Ala-Thr-Gln-Arg-Leu-Ala-Asn-Phe-Leu-Val-His-Ser-Ser-Asn-Asn-Phe-Gly-Ala-Ile-Leu-Ser-Ser-Thr-Asn-Val-Gly-Ser-Asn-Thr-Tyr-NH2 (disulfide bridge between cysteines 2 and 7) |
| CAS Number | 122384-88-7 |
| Molecular Weight | 3903.33 |
| Formula | C165H261N51O55S2 |
| Sequence | KC*NTATC*ATQRLANFLVHSSNNFGAILSSTNVGSNTY-NH2 |
| Modifications | C-terminal amide and a disulfide bridge between cysteines 2 and 7 |
Solubility and Storage
| Solubility | Soluble to 10 mg/ml in DMSO |
| Appearance | Freeze dried solid |
| Storage | Store dry, frozen and in the dark |
Batch Specific Data
| Purity | >95% by hplc |
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Recent citations
A new publication from the University of Ljubljana uses MCA-AVLQSGFR-Lys(Dnp)-Lys-NH2, the FRET substrate for the severe acute respiratory syndrome coronavirus main protease (SARS-CoV Mpro), to determine the inhibitory potential of plant polyphenols
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