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Related Experiment Video

Updated: May 15, 2026

Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain
09:00

Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain

Published on: April 28, 2022

Optimized protocol for amyloid-β extraction from the brain.

María Izco1, Pedro Pesini, Virginia Pérez-Grijalba

  • 1Araclon Biotech, Proteomic Laboratory, CIBIR, Logroño, Spain.

Journal of Alzheimer'S Disease : JAD
|January 11, 2013
PubMed
Summary

Standard Alzheimer's disease mouse model protocols may significantly underestimate amyloid-β (Aβ) levels. Optimizing extraction buffer volumes and performing multiple extraction steps are crucial for accurate Aβ quantification in brain tissues.

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Alzheimer's Disease Research

Background:

  • Amyloid-beta (Aβ) quantification in transgenic mouse models is vital for Alzheimer's disease (AD) research.
  • Current standard protocols for Aβ extraction involve sequential homogenization using various buffers.
  • The efficiency of these standard protocols in extracting total Aβ has not been thoroughly evaluated.

Purpose of the Study:

  • To investigate whether standard Aβ extraction protocols accurately quantify total Aβ in mouse brain tissues.
  • To determine if current methods lead to underestimation of Aβ burden.
  • To identify optimized procedures for more accurate Aβ measurement.

Main Methods:

  • Utilized standard tissue homogenization techniques for Aβ extraction from transgenic mouse brain samples.

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Full- versus Sub-Regional Quantification of Amyloid-Beta Load on Mouse Brain Sections
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Full- versus Sub-Regional Quantification of Amyloid-Beta Load on Mouse Brain Sections

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A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation
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A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation

Published on: March 27, 2017

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Last Updated: May 15, 2026

Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain
09:00

Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain

Published on: April 28, 2022

Full- versus Sub-Regional Quantification of Amyloid-Beta Load on Mouse Brain Sections
07:28

Full- versus Sub-Regional Quantification of Amyloid-Beta Load on Mouse Brain Sections

Published on: May 19, 2022

A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation
06:34

A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation

Published on: March 27, 2017

  • Varied extraction buffer volumes and the number of extraction repetitions (soluble and membrane-bound fractions).
  • Quantified Aβ levels using established biochemical assays.

    • Main Results:

    • Standard protocols demonstrated a significant underestimation of total Aβ content in brain tissues.
    • Increased extraction buffer volumes led to higher Aβ recovery.
    • Performing at least two sequential extraction steps for both soluble and membrane-bound Aβ fractions was necessary for comprehensive extraction.

    Conclusions:

    • Standard Aβ extraction protocols may not capture the full extent of Aβ accumulation in mouse models of AD.
    • Optimized extraction methods, including increased buffer volumes and multiple extraction cycles, are essential for accurate Aβ quantification.
    • Accurate Aβ measurement is critical for reliable interpretation of results in Alzheimer's disease research using animal models.