Proteomics - CD BioSciences




Proteomics studies the entire set of proteins in a biological system. By identifying proteins of interest, characterizing PTMs, and determining interacting partners, it contributes to understand the function of individual proteins and enables the determination of gene and cellular function at the protein level.

In the research of signaling pathways, it is the mainstay to identify proteins as novel regulators, characterize the proteins identified and dissect the mechanism of the regulation, a large part of which can be achieved by proteomics study.

Mass spectrometry (MS) is an analytical technique widely used for proteomics analysis. With the breakthroughs in MS technology, it allows new types of measurement and improves the quality of data.

Adapting the most advanced MS-based technologies, CD BioSciences offers a panel of solutions to enable broader and deeper analyses into the proteome.


MS-based Technologies for Proteomics

In a typical MS procedure, samples are first separated, then ionized, followed by mass analysis.

  • Separation

    Proteins usually co-exist with other proteins and molecules in the biological medium. Methods widely used for separation of proteins before MS analysis are two-dimensional gel electrophoresis (2D gel) which includes isoelectric focusing (IEF) and SDS-PAGE, and high-performance liquid chromatography (HPLC).

  • Ionization

    MS measures ionized analytes in the gas phase. Electrospray ionization (ESI) and matrix-assisted laser desorption/ionization (MALDI) are two primary techniques commonly used to volatilize and ionize the proteins or peptides for MS analysis.

  • Instrumental Configuration

    For mass analyzers, there are four basic types commonly used in proteomics research: ion trap (quadrupole ion trap/QIT, linear ion trap/LIT), time-of-flight (TOF), quadrupole (Q), Fourier-transform ion cyclotron resonance (FTICR or FT). These instruments can stand alone, or be "hybridized" to combine the advantage of different analyzers. The "hybrid" instruments include Q-Q-Q (triple quadrupole), QqLIT (triple quadrupole-linear ion trap), Q-TOF, TOF-TOF.

Instrumental Configuration Ionization Major Applications in Proteomics
  • Protein identification of low complex samples;
  • PTM identification
  • High-throughput large scale protein identification from complex peptide mixtures;
  • PTM identification
  • Quantification in SRM mode;
  • PTM detection;
  • Quantification in SRM mode;
  • PTM detection;
  • Protein identification from complex peptide mixtures;
  • Top-down proteomics;  
  • PTM identification
  • Top-down proteomics;
  • High mass accuracy PTM characterization
  • Protein identification from in-gel digestion
  • Protein identification from in-gel digestion

MS-based Solutions for Proteomics

Proteomics studies the features of proteins, which include but are not limited to expression, localization, interaction, structure, PTM and activity. A MS-based proteomics analysis can be achieved using either bottom-up (at intact protein level) or top-down (at the enzymatically digested peptide level) proteomics.

  • Protein Identification and Quantitation

    Proteomics studies gene and cellular function directly at the protein level. The mainstay of proteomics is protein and peptide identification.

    CD BioSciences provides MS analysis to sensitively identify and accurately quantify the components of a complex protein sample in a high-throughput manner.

  • PTM Characterization

    The function of most proteins is under the regulation of post-translational modifications, such as phosphorylation, acetylation, methylation, glycosylation, lipidation, nitrosylation and ubiquitination.

    CD BioSciences provides analysis to determine types of PTM and map PTM sites on individual protein subunits to understanding the function and regulation of proteins. You may also find our solution for PTM Enzymes helpful.

  • Structure Analysis

    Structure determines protein function. The primary structure of a protein is the linear amino acid sequence. The stable folding patterns (alpha helices and beta sheets) are known as the secondary structures of proteins. The tertiary structures of proteins are the ensemble of formations and folds in a polypeptide. And the quaternary structure of a protein refers to those macromolecules with multiple subunits.

    CD BioSciences provides MS analysis to study both primary and higher-order structures of proteins, including de novo (peptide) sequencing, peptide mapping, N-terminal sequencing analysis, C-terminal sequencing analysis.

  • Protein Interactions

    Protein-protein and protein-ligand interactions are the core of almost every cellular process and drug discovery project. The interactions are the basis of biological functions, from gene transcription to protein translation and signal transduction.

    CD BioSciences provides MS analysis to determine the interaction between proteins and with other molecules (e.g., proteins, DNAs, RNAs, hormones, lipids).

  • Protein Profiling

    Proteome is with considerable complexity, and should be characterized in some depth. Thus, large-scale and quantitative analysis of protein expression profiles is needed.

    CD BioSciences provides MS-based protein profiling to generate protein interactome (protein-protein linkage maps), and study protein stoichiometry by measuring the exact amounts of the individual components in protein complexes.

Relative Services


CD BioSciences offers cost-effect, high quality and hassle-free proteomics solutions to our clients worldwide. We guarantee to deliver our products and results on time. Please feel free to contact us.

For research use only. Not intended for any clinical use.