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    Mass Spectrometry Detection in Proteomics

      Mass spectrometry detection in proteomics is an advanced analytical technique widely used to analyze protein samples, offering both qualitative and quantitative information. This technology has become essential in proteomics, providing detailed insights into protein expression, modifications, and interactions.

       

      The core principle of mass spectrometry detection in proteomics involves the use of a mass spectrometer, which measures the mass-to-charge ratio (m/z) of ions. This allows the instrument to determine the molecular mass and infer the structure of proteins and peptides. Mass spectrometry works by measuring the different behaviors of ions in electric and magnetic fields, enabling the identification and quantification of proteins in complex biological samples. The typical steps in this process are:

       

      1. Sample Preparation

      Proteins are extracted from biological samples and digested into smaller peptides using enzymatic methods.

       

      2. Peptide Separation

      Peptides are separated by liquid chromatography, isolating them based on their physicochemical properties.

       

      3. Ionization

      Peptides are ionized, converting them into charged species that can be analyzed by mass spectrometry.

       

      4. Mass Analysis

      The mass spectrometer measures the mass-to-charge ratio (m/z) of the peptide ions and generates a mass spectrum that represents the distribution of ions.

       

      5. Data Analysis

      Specialized software is used to analyze the mass spectrum, identify peptide sequences, and deduce the identity of the parent proteins.

       

      Applications

      Mass spectrometry detection in proteomics has a wide range of applications, including:

       

      1. Protein Identification

      Identifying which proteins are present in a sample, including their isoforms and post-translational modifications.

       

      2. Protein Quantification

      Measuring the abundance of specific proteins across different samples, which is critical for understanding their role in various biological processes.

       

      3. Proteome Analysis

      Conducting comprehensive proteomic analyses of specific cells or tissues to reveal their complete protein composition.

       

      4. Protein-Protein Interactions

      Studying the interactions between proteins, which are fundamental to understanding cellular signaling and function.

       

      5. Post-translational Modification Analysis

      Identifying and characterizing modifications such as phosphorylation, glycosylation, and acetylation, which regulate protein activity and function.

       

      Workflow

      The workflow of mass spectrometry detection in proteomics involves the following steps:

       

      1. Sample Preparation

      Proteins are extracted from the biological source, purified, and digested into peptides for further analysis.

       

      2. Mass Spectrometry Analysis

      Liquid chromatography-mass spectrometry (LC-MS) is the technique of choice, where peptides are first separated and then analyzed by mass spectrometry.

       

      3. Data Processing and Analysis

      The raw mass spectrometry data is processed using specialized software to identify proteins and quantify their expression levels.

       

      MtoZ Biolabs, an integrated chromatography and mass spectrometry (MS) services provider.

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