Proteomics is a comprehensive and systematic analysis of protein identification and quantification from a macroscopic perspective.Together with the other “omics” technologies, such as genomics and transcriptomics, it assists in expounding the identity of proteins to reveal their expression, structure, functions, interactions and modifications.
Proteomics plays a crucial role in drug development. Characterizing the proteins of a cell, tissue or organism is highly useful in the identification of candidate biomarkers, bacterial antigens and possible immunohistochemistry markers targeted by the immune response and related to infectious or neoplastic diseases. In addition, by detecting the alteration of expression patterns in different diseases or in response to different treatments, proteomics can also explain distinct patient reactions during clinical intervention.
Novogene applies mass spectrometry (MS) technology by using the Thermo Q ExactiveTM HF-X mass spectrometer to achieve accurate mass determination and protein characterization, providing customers with unsurpassed data and excellent service.
The Novogene Advantage
- Comprehensive Analysis: Including quantitative, qualitative, post-translational modification and in-depth protein profiling.
- High Performance Platform: The Thermo Q ExactiveTM HF-X mass spectrometer guarantees high sensitivity and excellent stability in analysis quality.
- Extraordinary Informatics Expertise: Cutting-edge bioinformatics pipeline with internationally recognized best-in-class software, proving customers with publication-ready data.
Proteomics Service Overview
The qualitative analysis includes identification of proteins, protein interactions and protein modifications after collection from gel, as well as identification of the full spectrum proteome from tissue or blood.
Post-translational Modification Proteomics
Post-translational modification (PTM) of a protein is a biochemical process that increases the functional diversity of the proteome by enzymatically adding functional groups to
the protein following protein biosynthesis. Common modification types include phosphorylation, acetylation and ubiquitination, which change the molecular mass accordingly.
Mass spectrometry allows for protein modification to be quantified, thus enabling post-translational modifications to be analyzed qualitatively and quantitatively.
Protein quantitative analysis
Volcano diagrams of diﬀerential expression proteins
Hierarchical clustering heatmap
Protein domain enrichment histogram
KEGG enrichment scatter plot of diﬀerential expression proteins
GO enrichment DAG
Protein-protein interaction networks
Correlation analysis with transcriptome
- Venn diagram of expression regulation
- Correlation analysis of expression level
- GO enrichment correlation analysis
- GO enrichment clustering heatmap
Post-translational modiﬁcation analysis
- Motif analysis
- Clustering heatmap of phosphorylated kinases
Examples of Publications Using Novogene’s Expertise
|Microbiome, 5:14 (2017)||Gut microbiota dysbiosis contributes to the development of hypertension|
|Nature Communications,10:1639 (2019)||KIBRA controls exosome secretion via inhibiting the proteasomal degradation of Rab27a|