| Name
|
Amylin, Human, Amide
|
| Other Name
|
Diabetes-Associated Peptide (DAP), amide, humanInsulinoma or islet amyloid polypeptide (IAPP)
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| Sequence (Single letter abbreviations)
|
KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY-NH2
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| Sequence（Three letter abbreviations）
|
{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
|
| C-port
|
NH2
|
| Chemical bridge
|
Disulfide Bridge: Cys2-Cys7
|
| Basic description
|
Amylin, a 37-amino acid polypeptide that is structurally related to calcitonin, is secreted from the B cells of the pancreas. Amylin has anoretic effects in rats. Amylin may be responsible for the etiology of insulin resistance of type II diabetes mellitus through its modulation of peripheral effects of insulin. Amylin blocks the activation of glycogen synthase by insulin.
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| Solubility
|
Can be dissolved in DMSO or DMF first and then dilute with water
|
| The molecular weight
|
3903.280
|
| Chemical formula
|
C165H261N51O55S2
|
| The purity
|
> 95%
|
| Storage conditions
|
Store at -20°C. Keep container tightly closed. Store in a cool dry place.
|
| Annotation
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| Documents
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| Figures
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| Reference
|
Konarkowska B, et al. Thiol reducing compounds prevent human amylin-evoked cytotoxicity. FEBS J. Oct 2005; 272(19): 4949-4959.
Kajava AV, et al. The parallel superpleated beta-structure as a model for amyloid fibrils of human amylin. J. Mol. Biol. Apr 2005; 348(2): 247-252.
Guerreiro LH., etc. Polymeric particles for the controlled release of human amylin. Colloids Surf B Biointerfaces. 2012 Jun;94:101-6.
Kevin Hartman., etc. Bacterial curli protein promotes the conversion of PAP248-286 into the amyloid SEVI: cross-seeding of dissimilar amyloid sequences. PeerJ. 2013 Feb;12(1):e5.
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Amylin, Human, Amide
