Full spectrum of proteins

Full spectrum analysis refers to a protein component analysis, the object is the complete tissue, blood, body fluids, or its extracts, the aim is to identify the samples as much as possible of peptide and protein mixture components. Full spectrum analysis based on mass spectrometry, can provide high-throughput quantitative and modification analysis of protein for reference information. In addition, you can use the full spectrum analysis of the data and the transcriptome data combination, complement each other and mutual authentication gene annotations.

Differences in proteomics

Changes on the cell protein components in different periods, such as the differentially expressed proteins in different environment, to found that there were differences of protein types as the main target, is referred to as the difference of proteome study.

Differences in proteomics is a branch of proteomics studies structure, this kind of research, many proteomics researchers of in China  or abroad is increasingly attented, the main reason is as follows: first, the differences in proteomics research on technology of realizability is higher. Second, proteomics differences reflect the dynamic nature of the protein. Third, differences in proteomics has wide application prospect and clear.

Modification Proteomics

Post-translational modification is an important way to regulate protein function and the key regulatory mechanisms in the phenomenon of life. There are more than 20 common modification types.

Specially, phosphorylation is an important post-translational modification, related closely to signal transduction, cell cycle, growth and development as well as the mechanisms of cancer and many other biological problems. Because protein phosphorylation is dynamic and small in the amount, the phosphorylated peptides are difficult to be ionized in the mass spectrometry, and ion inhibited by non-phosphorylated peptides. We could identify more than 1000 phospholation-sites by using TiO2 protocol to enrich phosphor-peptides.

We could also measure a Histone modification map targeting many possible modification events/sites in the samples. 

Quantitative proteomics

Quantitative proteomics research accurate quantification for all expressed proteins of a whole genome or proteins in a complex mixed system. This concept indicates the constant improvement and perfection. Proteomics has transferred the research priorities from high-throughput protein identification to detecting the protein expression differentiation through relevant quantitative analysis to get proteins’ functional information.

Target proteomics

Multiple-reaction-monitoring (MRM) is a highly selective, sensitive, and robust assay to monitor the presence and amount of biomolecules. Depending on its high selectivity and sensitivity, it is being used in the verification of global proteomics data, the discovery of lower abundance proteins, protein post-translational modifications, discrimination of select highly homologous protein isoforms and as the final step in biomarker discovery.

Application Software of Protein

Mass spectrometry platform has more than 30 experienced design and development of professional technology and analysis of biological information, is mainly responsible for large-scale protein group data processing, analysis and deep development. Relying on high-performance computing platforms and self-developed data analysis software platform of BGI, the application of proteomic analysis of proprietary software Mascot, ProteinPilot, Proteome Discoverer, MRMPilot, MarkerView, MaxQuant, TPP, pFind, pLink, blast2go etc from SWISS PROT, TreEMBL, NCBI, Uniprot database of protein sequence analysis of protein structure analysis, annotation of protein, such as biological pathways analysis. For a large amount of data output, processing and analysis, provides technical support.