Resources
Proteomics Databases
Metabolomics Databases
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• Quantitative Proteomics in Cancer Research
Cancer, as a serious disease, significantly affects human health and quality of life. Early diagnosis and effective treatment of cancer are crucial for improving patient survival rates. In recent years, quantitative proteomics, as a powerful technique, has played an important role in cancer research. We will explore the use of quantitative proteomics in cancer research, focusing on its potential to identify biomarkers and therapeutic targets.
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• Comprehensive Analysis of Protein-Protein Interaction Verification Methods
MtoZ Biolabs is your optimum choice for protein-protein interactions services, with high-quality and efficient solutions. Proteins are among the most significant molecules in living organisms, playing various key roles within cells and controlling physiological processes within the organism. Furthermore, interactions between proteins, also known as protein-protein interactions, form the basis of cellular function networks.
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• Analyze the Dynamic Changes of Histone Modifications Using Mass Spectrometry
Histone modification is an important regulatory mechanism in cells, affecting gene expression by altering the structure and function of chromatin. Recent developments in mass spectrometry technology have allowed us to further investigate the dynamic changes in histone modification.
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• Protein Translation and Post-Translational Modification Detection Methods
Post-translational modifications (PTMs) are key biochemical processes in cells that modify the chemical properties, structure, function, and location of proteins. Common post-modification of proteins includes phosphorylation, acetylation, ubiquitination, glycosylation, pantothenylation, etc. Detecting these modifications is crucial for understanding the role and regulatory mechanisms of proteins. Below are the commonly used methods to detect protein post-translational modifications:
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• Profiling Cell Surface Proteins by Orbitrap Mass Spectrometry
Cell surface proteins hold a crucial position in life sciences, being key players in processes such as cell signaling, substance transport, immune response, cell recognition, and pathological processes. Understanding and characterizing the expression profiles of cell surface proteins is vital for elucidating cell functions and disease mechanisms.
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• 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.
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• 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.
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• 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).
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• 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.
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• 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.
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