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    Resources

    • • Quantitative Analysis of Cell Surface Proteins in Cancer Research

      Cancer research is a crucial area in modern biomedical science. Cell surface proteins play a key role in the onset, progression, and metastasis of cancer, serving as important molecular markers for cancer diagnosis, prognosis assessment, and targeted therapy. Therefore, the quantitative analysis of cell surface proteins in cancer cells is of great significance.

    • • Procedure for Enriching Cell Surface Proteins Using Biotin Affinity

      Cell surface proteins play critical roles in cellular interactions with the external environment, participating in signal transduction, transport, and cell recognition. Studying these proteins is not only essential for understanding fundamental cell biology but also has applications in drug development, disease diagnosis, and therapy.

    • • Quantitative Analysis of Peptides Using Parallel Reaction Monitoring

      In proteomics research, precise quantification of proteins is crucial for uncovering the molecular mechanisms underlying biological processes. Traditional protein quantification methods include isotope labeling techniques (e.g., SILAC, iTRAQ) and label-free quantification methods (e.g., DIA).

    • • Detection of Cell Surface Proteins via Biotin Affinity Purification

      Cell surface proteins play crucial roles in the exchange of materials, signal transduction, and cell recognition between cells and their environment. Studying these proteins is essential for understanding cellular communication, disease mechanisms, and drug target discovery. However, due to their low abundance and the complex membrane environment, isolating and identifying cell surface proteins can be challenging.

    • • Detection of Proteins Using Parallel Reaction Monitoring

      Parallel Reaction Monitoring (PRM) is a mass spectrometry (MS) technique used for the quantitative analysis of specific proteins or peptides in complex biological samples. As an alternative to Selected Reaction Monitoring (SRM), PRM employs high-resolution, high-mass accuracy mass spectrometers, often based on Orbitrap or Q-TOF systems.

    • • Principle of Molecular Weight Determination in Glycosylation Site Identification

      Biological drugs, as an important means of treating diseases, have drawn increasing attention. Among these complex protein drugs, glycosylation is a common post-translational modification that can affect the structure and function of drugs. Glycosylation sites, as specific amino acid residues that bind to sugar chains, play an important role in the stability, biological activity, and immunogenicity of drugs.

    • • Comprehensive Analysis of New Antigen Screening Processes

      Immunotherapy activates the patient's own immune system to actively attack cancer cells, bringing new hope for cancer patients. In personalized immunotherapy, the screening process for neoantigens is particularly important.

    • • New Strategies and Discoveries in Protein Disulfide Bonds via Mass Spectrometry

      "If each person's body is regarded as a bustling city, then proteins are the foundation that constructs this city." This is a commonly used praise for proteins. Within protein molecules, there is a special structure called a disulfide bond, which plays a crucial role in maintaining the stability and functionality of proteins.

    • • Mass Spectrometry Protein Analysis Revealing Protein Composition and Function

      Proteins within organisms are the fundamental elements that constitute cells and tissues, as well as the executors of various biological processes. Mass spectrometry (MS) protein analysis, as a powerful proteomics technique, can comprehensively and deeply analyze the composition and function of proteins, providing strong support for biological product development and disease research.

    • • How Does Endogenous Mass Spectrometry Source Affect Results?

      IP mass spectrometry is a technique that uses specific antibodies to identify and enrich specific protein complexes, and combines it with mass spectrometry analysis to identify the member proteins within the complex. This technique is widely used in biopharmaceutical research and disease studies, and careful consideration of the endogenous issues of the mass spectrometry source is necessary to obtain reliable results.

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