Based on comprehensive mass spectrometry facilities, Creative Proteomics provides you with a top-down approach to proteomics research. Direct top-down analysis of intact proteins, including post-translationally modified proteins and other large proteins, not just peptides.
Top-down MS enables both single protein analysis and protein complex characterization. And support both N-terminal and C-terminal sequencing services, especially when the ends of protein samples are modified and blocked. However, this method is mainly used for the comprehensive characterization of single proteins or mixtures of proteins of only low to moderate complexity, with rather low throughput. And the sensitivity and detection limit of mass spectrometers are poor for proteins, and most applications are limited to proteins smaller than 50 kDa.
Fig. 1 Multidimensional workflow in the top-down proteomics analysis. (Toby, T. K, et al., 2016)
Service Content of Top-Down Proteomics Analysis
Top-down proteomics strategies are used to characterize multiple intact proteins in a mixture. In top-down proteomics, intact proteins are first separated from complex biological samples by reversed-phase liquid chromatography and then directly ionized by electrospray ionization (ESI) or matrix-assisted laser desorption/ionization (MALDI) techniques. The resulting ions are fragmented by collision-induced dissociation (CID), high-energy collision-induced dissociation (HCD), electron capture dissociation (ECD), or electron transfer dissociation (ETD) and analyzed in tandem mass spectrometry. This method has great potential for protein identification, analysis, sequence analysis, and characterization of post-translational modifications.
Mass Spectrometry Facilities and Projects
- Tandem Mass Spectrometry (MS/MS)
- 2D Gel Electrophoresis with MS/MS
- Electrospray Ionization Mass Spectrometry (ESI-MS)
- Thermo Scientific™ Q Exactive™ HF Hybrid Quadrupole-Orbitrap Mass Spectrometer
- Matrix-Assisted Laser Desorption Ionization-Time of Flight Mass Spectrometry (MALDI-TOF MS)
Requirements for Samples
- We are able to accept almost all sample types.
- Please provide the specific concentration, volume, preparation time, and source of each sample. And inform the sample information as well as the control and experimental samples (if there is a group, describe the group information in detail.)
Deliverables
- Experimental steps
- Relevant mass spectrometry parameters
- Details of the identified phosphorylation sites
- Mass spectrometry images
- Raw data
Advantages of Top-Down Proteomics Analysis
- Less time consuming.
- Relatively simple sample preparation.
- No protein digestion required.
- Direct detection of the molecular weight of biological proteins.
- A large amount of information is retained, e.g., PTMs.
Service Process
As an industry leader, Creative Proteomics focuses on providing you with a top-down proteomics analysis service based on mass spectrometry facilities. If you are interested, please do not hesitate to contact us directly for a detailed discussion with our project experts.
Reference
- Toby, T. K.; et al. Progress in Top-Down Proteomics and the Analysis of Proteoforms. Annu Rev Anal Chem (Palo Alto Calif). 2016, 9(1): 499-519.
The service is for research only, not for clinical use.
