Peptides

Amylin (22-27) [NMeG24, NMeI26], human (IAPP) - 1 mg

$262.00
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  • Cat.Number : AS-61937
  • Availability :
    In stock

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This amino acids 22 to 27 fragment is a modification of the human islet amyloid polypeptide hIAPP (NFGAIL) with N-methylation of the amide bonds at G24 and I26. The introduction of two N-methyl rests in the amyloid-core-containing sequence NFGAIL converts this amyloidogenic and cytotoxic sequence into non-amyloidogenic and non-cytotoxic peptide. The peptide is able to bind with high-affinity full-length hIAPP and to inhibit its fibrillogenesis.

Specifications

Chemistry
Sequence one letter code
  • NF-(NMe-G)-A-(NMe-I)-L
Sequence three letter code
  • H-Asn-Phe-(NMe-Gly)-Ala-(NMe-Ile)-Leu-OH
Molecular Mass/ Weight
  • 661.8
Modification
Conjugation
  • Unconjugated
Quantity & Purity
Purity
  • Peak Area by HPLC ≥95%
Storage & stability
Form
  • Lyophilized
Storage Conditions
  • - 20 °C
Activity
Biomarker Target
Research Area
Sub-category Research Area
Usage
  • Research use
Source
Source / Species
  • human

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References

Design of a mimic of nonamyloidogenic and bioactive human islet amyloid polypeptide (IAPP) as nanomolar affinity inhibitor of IAPP cytotoxic fibrillogenesis

PNAS . 2006 Feb 14 ; 103(7) 2046 | DOI : https://doi.org/10.1073/pnas.0507471103

  • L. Yan
  • et al

Inhibition of hIAPP Amyloid-Fibril Formation and Apoptotic Cell Death by a Designed hIAPP Amyloid- Core-Containing Hexapeptide

Cell Press . 2005 Jul 01 ; 12(7) 797 | DOI : https://doi.org/10.1016/j.chembiol.2005.05.010

  • M. Tatarek-Nossol
  • et al

Structure-based design and study of non-amyloidogenic, double N-methylated IAPP amyloid core sequences as inhibitors of IAPP amyloid formation and cytotoxicity

J. Mol. Biol. . 2002 Jan 18 ; 315(3) 339 | DOI : https://doi.org/10.1006/jmbi.2001.5244

  • A. Kapurniotu
  • et al