The human genome is composed of 20,000-3,000 genomes, encoding more than 500,000 different proteins. More than 80% of proteins cannot work alone, usually in the form of protein-protein combination into complexes, participating in the regulation of the operation and mechanism of organisms. Interactions between proteins are part of cellular networks, and the basic structures in cells are similar. Current research demonstrates that cellular proteins can be coupled to large cellular protein interactions in ways that have an impact on cellular pathways. In gene regulation, proteins recognize chromosomal target DNA sites. Proteomics has grown tremendously in the past year, and many ways to identify and characterize protein interactions have been proposed. Mass spectrometry is one of the common methods of protein identification, which is used to detect genome-wide protein-protein interactions. Alfa Chemistry provides professional biotinylation services, focusing on the study of protein interactions, and can locate protein binding sites in a high-throughput and cost-effective manner.
Alfa Chemistry focuses on efficient in vivo biotinylation for efficient detection of protein interaction assays. The services we can provide include but are not limited to:
Over the years, a large number of methods have been developed for studying protein-protein interactions, and protein interaction databases have been developed for searching to identify interactions for a given bait protein. Alfa Chemistry focuses on providing a wide range of biotinylation strategies and methods, which can efficiently and accurately analyze protein interactions using confocal microscopy, co-immunoprecipitation, surface plasmon resonance (SPR) and spectroscopy research methods testing and characterization.
Protein interactions (PPIs) refer to the process by which two or more proteins bind together and are widely involved in biochemistry, quantum chemistry, molecular dynamics, metabolomics and genetics. Protein interactions are involved in the entire omics system of living cells and participate in important physiological processes such as DNA replication. The precise study of protein interactions can lead to insights into related diseases, which are expected to form the basis of recent therapeutic approaches. Researchers have developed methods for predicting protein-protein interactions, which can be used to determine the sites of protein binding and evaluate the coupling strength of protein interaction binding sites. While accurately predicting protein interaction interfaces and sites, the researchers also focused on predicting the drug-drug region of the binding site, providing a new guide for fragmented drugs.
Due to the rapid development of proteomics, more and more studies are used to efficiently detect protein-protein interactions. While developing new detection methods, it is also necessary to control costs and efficiently classify and count experimental data. In the future, more efficient detection methods can be used for refinement to detect protein-protein interactions with advanced technology and capabilities.
Alfa Chemistry uses a variety of characterization methods such as affinity labeling, affinity chromatography and co-precipitation to analyze the interaction of proteins in depth, so as to be suitable for high-efficiency proteomics research. If you are interested in our services, please contact us immediately.
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※ It should be noted that our service is only used for research, not for clinical use.
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