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Disulfide bond

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Disulfide bond is a covalent bond formed between the sulfur atoms of two cysteines. This bond is crucial for the stability and function of proteins, and many secreted proteins or proteins that are located at the cellular surface have formed disulfide bond to maintain the stability. To meet specific research needs of our customers, 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 developed a specialized platform, equipped with Q Exactive HF (Thermo Fisher), Orbitrap Fusion, and Orbitrap Fusion Lumos mass spectrometers, equipped with Nano-LC for disulfide bond analysis service. To better solve your research problems, we offer an all-inclusive service, including sample preparation, protein purification, digestion, peptide separation, LC-MS/MS analysis, pLink-SS software analysis and bioinformatics analysis. All you need to do is to tell us your project objective, and send us your cell/protein samples, and we will complete all the following experiments.

Service Workflow


• Mapping the disulfide bond sites of unknown proteins
• Verify the disulfide bonds and folding of protein samples

Key Features

• Analysis of proteins at single protein level and proteomics level
• High-throughput, quantitatively identify and analyze disulfide bridges of multiple proteins
• Protein are maintained and analyzed in native status

Sample Requirement

Note: Please use enough dry ice in the shipment, and choose express delivery to eliminate sample degradation.
We will perform testing experiment before we start official experiments. To ensure the most cost-effective and accurate analysis is provided, only qualified samples will proceed to the official analysis.


• Experiment procedures
• Parameters of liquid chromatography and mass spectrometer
• MS raw data files
• Peptide identifications and intensities
• Protein identifications and disulfide bonds mapping
Bioinformatics analysis

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