IMG-EN-AS-22819-01.jpg
Peptides

Beta-Amyloid (1-11) - 1 mg

$100.00
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  • Cat.Number : AS-22819
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    In stock

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Anionic interaction of Aß (1-11) with Factor XII is suspected to cause the massive activation of the C4 (Complement 4) system in cerebrospinal fluid of Alzheimer’s disease patients.

Specifications

Chemistry
Sequence one letter code
  • DAEFRHDSGYE
Sequence three letter code
  • H-Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-OH
CAS registry number
  • 190436-05-6
Molecular Formula
  • C56H76N16O22
Molecular Mass/ Weight
  • 1325.4
Modification
Conjugation
  • Unconjugated
Quantity & Purity
Purity
  • Peak Area by HPLC ≥95%
Storage & stability
Form
  • Lyophilized
Storage Conditions
  • - 20 °C
Activity
Research Area
Sub-category Research Area
Usage
  • Research use
Source
Source / Species
  • human

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Citations

Alkylated dihydroxybenzoic acid as a MALDI matrix additive for hydrophobic peptide analysis.

Anal Chem . 2012 Apr 16 ; 84(9) 4237 | DOI : 10.1021/ac300540r

  • Y. Fukuyama

Fibrillar amyloid beta-protein inhibits the activity of high molecular weight brain protease and trypsin.

J Alzheimer's Dis . 2005 Feb 01 ; 7(1) 37 | DOI : 10.3233/jad-2005-7105

  • Ved Chauhan

Improved β-Elimination-Based Affinity Purification Strategy for Enrichment of Phosphopeptides.

Anal Chem . 2003 Dec 15 ; 75(24) 6826 | DOI : 10.1021/ac034989u

  • D. McLachlin

References

Activation of complement and contact system in Alzheimer's disease

Mech Aging Dev . 2001 Nov 01 ; 122(16) 1971 | DOI : https://doi.org/10.1016/S0047-6374(01)00311-6

  • L. Bergamaschini
  • et al

Charge-based binding of complement component C1q to the Alzheimer amyloid beta-peptide

Am J Pathol . 1997 May 01 ; 150(5) 1531 | DOI : 9137079

  • S. Webster
  • et al

Fibrillar amyloid beta-protein inhibits the activity of high molecular weight brain protease and trypsin

Alzheimer’s Dis . 2005 Feb 01 ; 7(1) 37 | DOI : 10.3233/jad-2005-7105

  • Ved Chauhan
  • et al

Humoral Immune Response to Fibrillar β-Amyloid Peptide

Biochem . 2003 Sep 20 ; 42(40) 11682 | DOI : https://doi.org/10.1021/bi030100s

  • D. Miller
  • et al