IMG-EN-AS-60017-1-01.jpg
Peptides

Beta-Amyloid (11-40) - 1 mg

$473.00
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  • Cat.Number : AS-60017-1-
  • Availability :
    In stock

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Post-mortem Alzheimer’s diseased brain specimens reveal significant levels of Aß (11-40/42) within insoluble amyloid pools. The ß-secretase enzyme or ß-amyloid precursor protein-cleaving enzyme (BACE) generates the N terminus of Aß, ultimately leading to the production of full-length Aß (1-40/42) or truncated Aß (11-40/42). The abundance of Aß (11-40/42) produced by BACE suggests that their roles in AD pathogenesis may be important.

Pyroglutamyl (pGlu) peptides may spontaneously form when either Glutamine (Q) or Glutamic acid (E) is located at the sequence N-terminus. The conversion of Q or E to pGlu is a natural occurrence and in general it is believed that the hydrophobic γ-lactam ring of pGlu may play a role in peptide stability against gastrointestinal proteases. Pyroglutamyl peptides are therefore considered a normal subset of such peptides and are included as part of the peptide purity during HPLC analysis.

Specifications

Chemistry
Sequence one letter code
  • EVHHQKLVFFAEDVGSNKGAIIGLMVGGVV
Sequence three letter code
  • H-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-Gly-Val-Val-OH
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

β-Secretase Processing in the Trans-Golgi Network Preferentially Generates Truncated Amyloid Species That Accumulate in Alzheimer’s Disease Brain

J Biol Chem . 2002 May 01 ; 277(18) 16278 | DOI : https://doi.org/10.1074/jbc.M111141200

  • J.T. Huse
  • et al

Glu11 Site Cleavage and N-Terminally Truncated Aβ Production upon BACE Overexpression

Biochem . 2002 Feb 08 ; 41(9) 3128 | DOI : https://doi.org/10.1021/bi015800g

  • K. Liu
  • et al

Processing Amyloid Precursor Protein at the β-Site Requires Proper Orientation to Be Accessed by BACE1

J Biol Chem . 2004 Sep 01 ; 279(37) 3910 | DOI : https://doi.org/10.1074/jbc.M407101200

  • I. Qahwash
  • et al