Proteomics
Overview
The term “Proteome”, coined in the 1990’s, describes the entire protein content in a cell, tissue, or bodily fluids, at any given time. Proteomics is thus defined as the global study of proteins. At the CPGR, this includes the investigation of protein structure, expression and interaction on a system-wide scale.
Proteomics at the CPGR
The task of studying the Proteome comes with a unique set of challenges. One is based on the sheer number of proteins that can, in principle, be identified. The 23,000 genes in the human genome can code for at least ten times as many proteins; in extreme cases a single gene alone can code for over 1,000 proteins. Additionally, there’s a dynamic range of proteins found in biological samples, as well as numerous post-translational modifications.
Proteomic technologies play a key role in discovery approaches in the post-Genomics era. Based on the advances that have been made in the field of mass spectrometry (MS) in particular, MS-based biomarker discovery plays an increasingly critical role in diagnostics and drug development.
- Discovery Proteomics
- Targeted Proteomics
- Protein Identification
- Proteomics Price Structure
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Mass Spectrometry-based expression Profiling
- Isobaric Labelling
Quantification of relative and absolute amounts of protein from different sources in one experiment - Label-Free Protein Profiling
Identification of regulated proteins by relative quantitation
Contact the Proteomics Manager to discuss your needs.
Complex or simple protein mixtures
- Protein identification based on the molecular masses of peptides derived from a digested protein
- Protein Identification by LC-MS/MS, protein identification by precursor peptide fragmentation following protein digestion with trypsin
- Phosphopeptide enrichment, study enzyme activation or inactivation, cell signalling and protein-protein interactions through phosphorylated peptides
- Phosphoprotein identification
For us to provide you with an accurate quotation, please complete a simple questionnaire for us.
Below is a guideline for standard workflow procedures but please do contact us to confirm an accurate quote for the work you require.
Standard assay list | Description | Local Academic | Commercial Rates |
Protein ID 120 min run time on a Thermo Q-Exactive (min. of 20 samples) | 120 min LC-MS/MS runs Q Exactive Orbitrap | R 1,600 | R 2,300 |
Protein ID 60 min run time on a Thermo Q-Exactive (min. of 20 samples) | 60 min LC-MS/MS runs Q Exactive Orbitrap | R 800 | R 1,200 |
Label free protein quantitation, 120 min run time on a Thermo Q-Exactive (min. of 20 samples) | Label free quantification with 120 min LC-MS/MS runs | R 2,000 | R 2,600 |
Label free protein quantitation, 60 min run time on a Thermo Q-Exactive (min. of 20 samples) | Label free quantification with 60 min LC-MS/MS runs | R 1000 | R 1,400 |
iTRAQ label based protein quantitation, no fractionation | iTRAQ Profiling on Q Exactive | * | * |
iTRAQ label based protein quantitation, IEF 12 lane fractionation | iTRAQ Profiling on Q Exactive | * | * |
iTRAQ label based protein quantitation, IEF 24 lane fractionation | iTRAQ Profiling on Q Exactive | * | * |
Phosphoproteomic analysis | * | * | |
Sample preparation – In-solution digest (min. of 20 samples) | R 300 | R 400 | |
Sample preparation – In-gel digest (min. of 30 samples) | R 300 | R 400 | |
Labour/Consultation | Additional labour | R 500/h | R 800/h |
Bioinformatics/Consultation | Data analysis | R 700/h | R 1,400/h |
*Please contact us to discuss your needs and possible pricing outcomes