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Related Concept Videos

Sample Preparation for Analysis: Overview01:21

Sample Preparation for Analysis: Overview

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Sample preparation is an essential step in the analytical process. It involves preparing a sample so that it can be analyzed accurately. The goal is to extract the analyte, the substance you want to measure, from the sample while removing any components that may interfere with the analysis. Sample preparation techniques vary depending on the physical state of the sample.
Bulk or large solid samples are typically reduced in size using grinding, crushing, or milling techniques to increase the...
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Sample Preparation for Analysis: Advanced Techniques01:08

Sample Preparation for Analysis: Advanced Techniques

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Accurate analysis of complex samples often requires advanced preparation techniques to achieve reliable and reproducible results. Samples containing inorganic or organic materials can be challenging to dissolve or decompose effectively. Standard sample preparation methods include acid digestion, fusion, dry ashing, and wet digestion.
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Passive Filters01:27

Passive Filters

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Passive filters are utilized to shape the frequency spectrum of signals across a diverse array of applications. These filters, using only passive elements like resistors (R), inductors (L), and capacitors (C), are capable of selectively allowing or blocking certain frequency ranges without the need for external power sources.
Low-Pass Filters
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Active Filters01:25

Active Filters

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Active filters are electronic circuits that use operational amplifiers (op-amps), resistors, and capacitors to filter out unwanted frequency components from a signal. A first-order low-pass active filter is designed to pass signals with a frequency lower than a certain cutoff frequency and attenuate frequencies higher than that cutoff frequency. The transfer function for a first-order low-pass active filter is:
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Preparation of Samples for Electron Microscopy01:20

Preparation of Samples for Electron Microscopy

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To be visualized by an electron microscope, either transmission or scanning, biological samples need to be fixed (stabilized) so the electron beam does not destroy them and dried thoroughly (desiccated/dehydrated) so the vacuum does not affect them. Fixation needs to be done as quickly as possible because the sample properties will start changing as soon as it is removed from its natural environment. For example, in a tissue sample, the oxygen levels begin decreasing, causing an altered...
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Proteomics01:33

Proteomics

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A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
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Proteomic Sample Preparation from Formalin Fixed and Paraffin Embedded Tissue
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Filter-Aided Sample Preparation for Proteome Analysis.

Jacek R Wiśniewski1

  • 1Biochemical Proteomics Group, Department of Proteomics and Signal Transduction, Max-Planck Institute for Biochemistry, Martinsried, Germany. jwisniew@biochem.mpg.de.

Methods in Molecular Biology (Clifton, N.J.)
|September 28, 2018
PubMed
Summary
This summary is machine-generated.

Filter-aided sample preparation (FASP) enhances proteomic analysis by efficiently extracting proteins and generating high-yield peptides. This method improves protein identification and sequence coverage for diverse sample sizes.

Keywords:
Bottom-up proteomicsFilter-aided sample preparation (FASP)Multienzyme digestion FASPProtein digestionProteomic reactorProteomic sample preparationSample preparation

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Area of Science:

  • Proteomics
  • Biochemistry
  • Analytical Chemistry

Background:

  • Quantitative protein extraction and high-yield peptide generation are crucial for bottom-up proteomics.
  • Existing methods may face challenges with sample complexity and yield.

Purpose of the Study:

  • To present Filter-Aided Sample Preparation (FASP) as an effective method for proteomic sample processing.
  • To demonstrate FASP's capability for detergent removal, protein digestion, and peptide isolation.

Main Methods:

  • Utilized disposable centrifugal ultrafiltration units for sample processing.
  • Employed sequential digestion with two or three proteases.
  • Processed samples ranging from micrograms to milligrams of total protein.

Main Results:

  • Achieved efficient detergent depletion and peptide isolation.
  • Generated peptide fractions with minimal overlap through multi-protease digestion.
  • Significantly increased the number of protein identifications and protein sequence coverage.

Conclusions:

  • FASP is a robust and versatile method for bottom-up proteomic analysis.
  • The technique is suitable for a wide range of biological sample quantities.
  • FASP improves the depth and quality of proteomic data.