| Bioactivity | Amylin (8-37) (human) (hIAPP (8-37)) is a 8-37 fragment of human islet amyloid polypeptide (IAPP). The duplex folding structure in the Amylin (8-37) (human) assembly has a hairpin structure[1]. |
| Invitro | Human islet amyloid polypeptide (hIAPP, amylin) is a major component in pancreatic amyloid deposits. Human IAPP with 37 amino acid residues is known to form soluble aggregates that further assemble into protofibrils and mature fibrils and eventually develop into plagues, and many studies have been conducted to identify the core regions with amyloidogenic properties. The assembly structures of Amylin (8-37) (human) (hIAPP (8-37)) shows lamella structures. The C terminal strands of Amylin (8-37) (human) peptides are stabilized by the coassembly molecule 4Bpy[1]. |
| Name | Amylin (8-37) (human) |
| CAS | 309244-90-4 |
| Shortening | ATQRLANFLVHSSNNFGAILSSTNVGSNTY |
| Formula | C138H215N41O46 |
| Molar Mass | 3184.43 |
| Transport | Room temperature in continental US; may vary elsewhere. |
| Storage | Please store the product under the recommended conditions in the Certificate of Analysis. |
Amylin (8-37) (human)
CAS: 309244-90-4 F: C138H215N41O46 W: 3184.43
Amylin (8-37) (human) (hIAPP (8-37)) is a 8-37 fragment of human islet amyloid polypeptide (IAPP). The duplex folding st
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