Post-Translational Modifications Proteomics Service
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.
Analysis Workflow
PTMs Analysis Service Categories
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.
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.
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.
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.
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.
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 Submission 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.
Deliverables
1. Experiment Procedures
2. Parameters of Liquid Chromatography and Mass Spectrometer
3. MS Raw Data Files
4. Identification of PTM Modified Peptides
Related Services
Protein Analysis
Protein Identification
Protein Mass Measurement
LC-MS Analysis of Pull-Down Proteins
Native MS Analysis
Protein Sequencing
Protein De Novo Seq
N-Terminal Sequencing
C-Terminal Sequencing
Edman Degradation
Protein Full-Length Sequencing
PTM Analysis
Phospho Proteomics
Acetyl Proteomics
Ubiquitin Proteomics
Glyco Proteomics
Disulfide Bond
Histone Modifications
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• Protein Lactylation Modification Analysis Service
In cell biology and biochemistry, post-translational modifications (PTMs) critically influence the stability, activity, localization, and functions of proteins. Among these, lactylation stands out as a significant PTM. This modification can occur on any protein residue with a free amino group, such as lysine, arginine, and tyrosine. During this process, lactate reacts with these amino acids to form an ester linkage, thereby altering protein structure and function.
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• Quantitative Tyrosine Phosphoproteomics Analysis Service
Protein phosphorylation is a common post-translational modification in eukaryotes. Eukaryotic cell protein phosphorylation is divided into two types: serine (Ser)/threonine (Thr) phosphorylation and tyrosine (Tyr) phosphorylation. Although the proportion of Tyr phosphorylation is small, it plays an extremely important role in the fate of cells and individuals, and is closely related to diseases such as cancer.
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• S-Nitrosylation Analysis Service
S-nitrosylation (SNO) is the covalent attachment of some nitroso (NO) groups to sulfhydryl residues (S) in proteins, forming S-nitrosothiols (SNOs). These groups are subsets of specific cysteine residues, leading to the formation of S-nitrosylated proteins. SNOs have a short half-life in the cytosol due to various reductases, such as glutathione (GSH) and thioredoxin, which act to remove the nitroso groups.
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• Quantitative Acetylomics Service
Acylation is a post-translational modification involving the attachment of acyl groups, such as acyl-CoA, to proteins. This modification plays a pivotal role in regulating key biological processes including epigenetics, energy metabolism, protein trafficking, and molecular interactions. Acylation research is a dynamic field in life sciences, with studies expanding beyond acetylation to include propionylation, malonylation, glutarylation, succinylation, and crotonylation.
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• Multipathway Phosphoproteomics Service
Protein phosphorylation is a reversible post-translational modification where amino acid residues in proteins are phosphorylated by kinases, which attach covalently bonded phosphate groups. This modification alters proteins' conformation, potentially activating, deactivating, or changing their functions. Research into protein phosphorylation enhances our understanding of biological processes and helps to define the mechanisms of diseases linked to abnormal phosphorylation levels.
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• Protein Sumoylation Identification Service
Small ubiquitin-like modifier (SUMO) is a post-translational modification of proteins that refers to the covalent attachment of a small ubiquitin-associated modifier to a protein. Unlike ubiquitination, which targets proteins for degradation, sumoylation modulates protein function across several cellular processes including nucleocytoplasmic transport, transcription regulation, apoptosis, protein stability, stress response, and cell cycle progression.
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• Protein Oxidative Modification Analysis Service
Protein oxidative modifications are generally induced by reactive oxygen species (ROS) such as superoxide anions, hydrogen peroxide, and hydroxyl radicals. These ROS are generated through multiple pathways in living organisms, including mitochondrial respiration, enzymatic redox reactions, and exposure to radiation. While protein oxidative modification is a natural physiological process, excessive ROS production or insufficient removal can cause excessive oxidation
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• Quantitative Methylomics Service
Methylation represents one of the most prevalent post-translational modifications, chiefly affecting transcription factors and histones, though it also modifies a subset of cytoplasmic proteins. This modification includes monomethylation, symmetric/asymmetric dimethylation, and trimethylation on arginine (R) and lysine (K) residues. Arginine methylation plays critical roles in RNA processing, gene transcription,
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• Protein Deamidation Modification Analysis Service
Protein deamidation involves the conversion of amide groups (-CONH2) in amino acids like glutamic acid and aspartic acid into their corresponding acids, α-ketoglutarate and glutamic acid, by losing an ammonia molecule (NH3). This non-enzymatic post-translational modification is crucial for understanding proteins' charge distributions, functions, stability, and interactions with other molecules, as well as their roles in diseases.
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• Top-Down PTMs Analysis Service
Top-down mass spectrometry (TDMS) is highly effective for comprehensive analysis of protein post-translational modifications (PTMs) because it evaluates intact proteins or peptides without requiring hydrolysis. This method is particularly valuable in the analysis of biopharmaceutical proteins, such as monoclonal antibodies and recombinant proteins, where it preserves many unstable modifications that are often lost during collision-induced dissociation (CID) cleavage in shotgun approaches.
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