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PTMs Identification

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Overview

Post-translational modifications (PTMs) are covalent and usually enzymatic modifications on proteins. Common PTMs include phosphorylation, acetylation, ubiquitination, glycosylation, and so on. These PTMs can cause huge influences on protein structure, distribution, and function, hence, increasing the complexity of proteome to a greater extent. Protein PTMs is generally analyzed by measuring the mass increased on the modified peptides. Since PTMs are generally present in very low abundance, specific enrichment procedures are required before PTMs identification. MtoZ Biolabs has established a powerful and professional PTMs analysis platform, which includes Thermo Fisher Q ExactiveHF and Obitrap Fusion Lumos mass analyzer system, coupled with Nano-LC system. Our aim is to provide the most professional support for our clients’ research.

Workflow of PTMs Identification Service

PTMs analysis service categories:

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Phospho-proteomics

MtoZ Biolabs provides protein phosphorylation analysis service with highly efficient phospho-peptides enrichment processing and Nano LC-MS/MS analysis. Coupled with SILAC/iTRAQ labeling, this service can be applied to large-scale phospho-proteomics analysis.

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Acetyl-proteomics

MtoZ Biolabs provides precise acetyl-proteomics analysis service using Nano LC-MS/MS. We also use CST acetylation-specific antibodies for acetyl-peptide enrichment, and 2-3 different enzymes for protein digestion to ensure full scan of acetyl-peptides.

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Ubiquitin-proteomics

MtoZ Biolabs offers protein ubiquitination identification and quantification service using high-resolution mass spectrometry analysis. We also use highly specific ubiquitin antibody for enrichment of low abundance ubiquitin-peptide.

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Glyco-proteomics

MtoZ Biolabs utilizes the HCD/ETD mode of Orbitrap Fusion mass spectrometry for glycoprotein analysis. Coupled with Byonic software, we can accurately analyze N- and O-linked glycosylation sites and the corresponding glycogens.

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Disulfide Bond Analysis

MtoZ Biolabs provides disulfide bond analysis service at both single protein level and proteome level. We have optimized our sample preparation method to reduce the chance of in vitro disulfide bond exchange and maintain the native protein structure to the greatest extent.

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Histone Modification Analysis

MtoZ Biolabs has optimized our sample preparation protocols to obtain highly purified histones with the least effect to the modification, and ensures precise histone modification analysis using Nano LC-MS/MS.


*Note: We also provide custom analytical service to identify many other types of PTMs. For special requirement, please contact us for project discussion.

Sample requirements

Format Liquid and Gel samples are acceptable.
Quantity A total of 5-10 ug proteins are required. Protein sample <5 ug can also be analyzed for specific types of PTM. Please contact us for special requirement.
Purity Detergents, such as SDS and salt should be as low as possible, especially for low amount of sample.
Note All reagents/solvent used must be of the highest purity to reduce contaminating substances. Samples should be handled with extreme caution and always in clean condition. Any source that may introduce contaminating proteins should be eliminated.

*Customers are welcome to contact us for detailed sample requirements before sending your samples.

Case Study

In this study, the ubiquitination modification sites of a Co-IP protein sample are analyzed. Part of the final analytical results is listed as below, showing the peptide sequences and identified ubiquitination sites respectively.

Reports

• Experiment procedures
• Parameters of liquid chromatography and mass spectrometer
• MS raw data files
• Identification of PTM modified peptides

Address:
155 Federal Street, Suite 700, Boston, MA 02110, USA
Email:
info@MtoZ-Biolabs.com
Tel:
1-857-928-2754