Creative BioMart offers you direct isolation and analysis of a wide range of MHC-associated peptides that play a role in the discovery, selection and prediction of multiple immunogenic epitopes, based on years of experimental experience and strong biochemical analysis capabilities.

Introduction of Isolation and Analysis of MHC-associated Peptides

Peptide antigens bind to MHC-encoded molecules and are presented on the cell surface to form target molecules for T lymphocytes. This critical aspect of the adaptive immune system can help eliminate pathogen-infected cells and cancer cells and produce antibodies. The establishment of methods for the isolation and analysis of MHC-associated peptides has important research implications for tumor diagnosis and immunotherapy.

The analysis of MHC-associated peptides by data-dependent analytical mass spectrometry (MS) has led to groundbreaking knowledge of peptide binding to MHC molecules. Thanks to the amazing advances in MS-based technology over the past decade, hundreds of thousands to thousands of MHC-associated peptides can now be analyzed in a single measurement using best-in-class biological modeling systems, and targeted analytical techniques have become a reliable method for accurately and reproducibly quantifying the dynamics of antigenic expression.

Our Choices of Isolation and Analysis of MHC-associated Peptides

We offer specialized equipment and state-of-the-art technology to advance peptide-associated projects related to MHC. Our services include peptide generation using protease hydrolysis, peptide isolation by immunoaffinity chromatography (reversed-phase HPLC, RP-HPLC), and peptide analysis of interest by sequencing or LC-MS/MS.

We have introduced the following suitable methods as solutions for the isolation and analysis of MHC-associated peptides.

• Acid elution from whole-cell lysate

Acid elution is a commonly used method for the identification and isolation of MHC-associated peptides. We provide the method primarily uses trifluoroacetic acid to elute MHC class I and class II peptides from whole cell solutions with strong acid.

• Acid elution from the cell surface

Another type of acid elution is a mild acid elution that releases MHC class I peptides (not class II peptides) from the cell surface. After elution, the peptides are concentrated mainly on cation exchange or reversed-phase columns before further analysis. Our acid elution has distinct advantages in terms of simplicity of operation, cost-effectiveness and the acquisition of cell surface MHC peptides that are primarily the relevant fraction for T cell recognition.

• Immunoaffinity purification

Immunoaffinity separations are purified from detergent solubilized cytolytic acids by releasing class I and class II MHC peptide complexes based on immunoaffinity. We utilize antibodies immobilized on a solid support matrix as ligands to specifically isolate and purify proteins and protein complexes. And they can be used to analyze unmodified and post-translationally modified MHC-associated peptides. Therefore, it is of central importance in MHC peptide isolation.

Advantages of Creative BioMart

• High isolation specificity
• High detectable levels of MHC- associated peptides
• Flexibility in isolation and analysis
• Cost saving and fast delivery

Turnaround Time

Our MHC peptide isolation and sequence analysis workflow allows peptides to be transferred directly from the RP-HPLC system to MS for fragmentation analysis. Project turnaround time depends on your research sample parameters. The identification, isolation and analysis of MHC peptides are essential for gaining insight into the fundamental rules of immune recognition and for developing innovative immunotherapeutic approaches against cancer and other diseases.

Creative BioMart offers a comprehensive service at every stage of project development, with years of experience in MHC-associated peptide research, including T-cell epitope (MHC-associated peptide) isolation and analysis, to present you with the best product and most complete analysis report. If you are interested in our services, please contact us for more detailed information.

Reference

• Etienne. C, et al. (2015). Analysis of major histocompatibility complex (MHC) immunopeptidomes using mass spectrometry. Molecular and Cellular Proteomics. 14(15), 3105-3117.