MS-Based Protein Interaction Identification Service

    Interacting protein mass spectrometry identification is a method utilizing mass spectrometry technology to study protein-protein interactions. It separates target protein complexes through methods such as immunoprecipitation (IP), affinity purification (AP), etc. Then, it employs protein enzymatic digestion to generate peptide fragments, followed by liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis of these peptides. Finally, based on the mass spectrometry data, combined with bioinformatics tools, it identifies and quantifies interacting proteins. Interacting protein mass spectrometry identification can identify or verify interacting proteins, discover new proteins interacting with target proteins, identify and quantify interacting proteins, and elucidate protein signaling pathways in organisms, aiding in drug target discovery and biomarker research, and providing a basis for drug development.


    MtoZ Biolabs provides one-stop interacting protein mass spectrometry identification services based on Thermo Fisher's Orbitrap Exploris 240 mass spectrometry platform combined with Nano-LC chromatography. This service analyzes the mass spectrometry identification of proteins/protein mixtures in IP, Co-IP samples, GST fusion protein Pull-down, and other purified samples. The protein sample pre-processing in the identification experiment strictly follows the article published in Nature Methods: "Universal sample preparation method for proteome analysis," ensuring higher peptide coverage in the identification experiment.


    Analysis Workflow

    1. Protein Extraction

    Optimal methods are employed to extract proteins from cell or tissue samples, and the purity and concentration of proteins are determined to ensure the quality of the extract.


    2. Interacting Protein Acquisition

    Target proteins and their interacting proteins are enriched using IP, GST-Pull-down, or immunoblotting methods according to experimental requirements.


    3. Elution and Enrichment

    Target protein complexes are eluted from the binding medium, enriched, and protein samples are collected for the subsequent mass spectrometry analysis.


    4. Protein Digestion

    The eluted interacting protein complex samples are enzymatically digested with various proteases (such as trypsin) to generate peptide fragments.


    5. Peptide Separation and Purification

    Peptide fragments obtained after digestion are separated and purified using high-performance liquid chromatography (HPLC) or reversed-phase high-performance liquid chromatography (RP-HPLC) techniques.


    6. Mass Spectrometry Analysis

    Peptide fragments are subjected to mass spectrometry analysis via LC-MS/MS to obtain mass spectrometry data.


    7. Data Processing and Analysis

    Mass spectrometry data is subjected to database searches and bioinformatics analysis for qualitative and quantitative identification of interacting proteins.


    Service Advantages

    1. High Sensitivity and Accuracy

    Our mass spectrometry technology accurately detects interacting proteins even in complex biological samples, including low-abundance interacting proteins, with high sensitivity.


    2. High Throughput

    Mass spectrometry technology can identify and quantify a large number of proteins in a short time, saving researchers time and experimental costs.


    3. Diverse Protein Interaction Types

    Our services cover various protein interaction types, including homologous interaction, heterologous interaction, transient interaction, permanent interaction, and among others.


    4. Relative Unbiasedness

    Compared to traditional techniques like gene chips and yeast two-hybrid, mass spectrometry technology exhibits relatively low bias in detecting protein interactions.


    5. Versatility

    Mass spectrometry technology can be applied to various biological systems, including bacteria, yeast, plants, animals, and humans, supporting research in multiple biological fields.


    6. Rich Structural Information

    Mass spectrometry technology provides comprehensive structural information on proteins, including post-translational modifications, cleavage, and protein-protein interactions, aiding researchers in understanding protein function and regulation mechanisms.


    Sample Submission Requirements

    1. Total Protein Extract

    Can be extracted from cells, tissues, or organisms. It is recommended to provide at least 100 µg of protein to ensure experimental success.


    2. Enriched Proteins

    For the identification of specific target protein interacting proteins, you can provide purified samples such as IP, Co-IP, and GST fusion protein Pull-down. It is recommended to provide at least 50 µg of enriched protein.



    In the technical report, MtoZ Biolabs will provide you with a detailed report, including:

    1. Experimental Procedures

    2. Relevant Mass Spectrometry Parameters

    3. Detailed Information on Interacting Protein Mass Spectrometry Identification

    4. Mass Spectrometry Images

    5. Raw Data

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