18285134. METHOD FOR CREATING CALIBRATION CURVE AND METHOD FOR MEASURING AMYLOID ß-RELATED PEPTIDE simplified abstract (SHIMADZU CORPORATION)

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METHOD FOR CREATING CALIBRATION CURVE AND METHOD FOR MEASURING AMYLOID ß-RELATED PEPTIDE

Organization Name

SHIMADZU CORPORATION

Inventor(s)

Naoki Kaneko of Kyoto-shi (JP)

METHOD FOR CREATING CALIBRATION CURVE AND METHOD FOR MEASURING AMYLOID ß-RELATED PEPTIDE - A simplified explanation of the abstract

This abstract first appeared for US patent application 18285134 titled 'METHOD FOR CREATING CALIBRATION CURVE AND METHOD FOR MEASURING AMYLOID ß-RELATED PEPTIDE

Simplified Explanation

The patent application describes a method for quantifying amyloid β-related peptide using mass spectrometry and immunoprecipitation techniques.

  • Providing standard solutions with varying concentrations of amyloid β-related peptide and a surfactant.
  • Mixing internal standard peptide with each standard solution.
  • Performing immunoprecipitation and mass spectrometry on calibration curve solutions.
  • Standardizing signal intensity of amyloid β-related peptide with internal standard peptide.
  • Calculating a regression equation of a calibration curve based on normalized intensities and peptide concentration.

Potential Applications

This technology can be applied in the field of Alzheimer's disease research for accurately quantifying amyloid β-related peptide levels in biological samples.

Problems Solved

This technology solves the problem of accurately measuring amyloid β-related peptide concentrations, which is crucial for understanding the progression of Alzheimer's disease and developing potential treatments.

Benefits

The benefits of this technology include improved accuracy and sensitivity in quantifying amyloid β-related peptide levels, which can lead to better insights into the pathophysiology of Alzheimer's disease.

Potential Commercial Applications

A potential commercial application of this technology could be the development of diagnostic tools for Alzheimer's disease based on quantifying amyloid β-related peptide levels in patient samples.

Possible Prior Art

One possible prior art could be existing methods for quantifying amyloid β-related peptide levels in biological samples using mass spectrometry techniques.

Unanswered Questions

== How does this method compare to existing techniques for quantifying amyloid β-related peptide levels? This article does not provide a direct comparison to existing techniques for quantifying amyloid β-related peptide levels.

== What are the limitations of this method in terms of sample size and processing time? This article does not address the limitations of this method in terms of sample size and processing time.


Original Abstract Submitted

Included is the steps of providing a plurality of standard solutions containing amyloid β-related peptide and a surfactant and having different concentrations of the amyloid β-related peptide; mixing a solution containing internal standard peptide with each of the plurality of standard solutions; performing immunoprecipitation and mass spectrometry on a plurality of calibration curve solutions; standardizing signal intensity (A) in the amyloid β-related peptide with the signal intensity (B) in the internal standard peptide for each of the plurality of calibration curve solutions; and calculating a regression equation of a calibration curve based on a plurality of normalized intensities and the concentration of the amyloid β-related peptide.