Leveraging breakthrough technologies to map linear, conformational and discontinuous epitopes with amino acid level resolution
A revolutionary technology that generates free radicals from a
plasma for Protein Footprinting. PLIMB is used for analyzing
protein structure and interactions with unprecedented degree of
speed, resolution and accuracy.
High Resolution Epitope Mapping
Antibody Aggregation Analysis
Epitope-Based Screening
Epitope Target Identification
High Resolution Epitope Mapping
Antibody Aggregation Analysis
Epitope-Based Screening
Epitope Target Identification
PLIMB is a revolutionary technique that provides high resolution data on the native, in-solution structure of the therapeutic and target antigen in a rapid analysis that is applicable to a wide range of proteins.
Immuto utilizes a mass spectrometry-based protein footprinting technique called Hydroxyl Radical Footprinting (HRF)- a powerful, validated method for studying protein structure, dynamics and interactions. For HRF, side chain residues of proteins in solution are labeled with hydroxyl (OH) radicals. The labeled regions are localized and quantified using mass spectrometry. For epitope mapping, the labeling of an antibody bound vs unbound samples are compared to identify the epitope and paratope regions. At Immuto, we use our proprietary Plasma Induced Modification of Biomolecules (PLIMB) technology for HRF studies. The instrument generates controlled doses of radicals from an atmospheric-pressure plasma to irreversibly label the solvent-accessible regions of proteins in solution. PLIMB is a fully automated, high throughput HRF system that can label samples in a 96-well plate. The instrument has an integrated radical detection and feedback system to precisely control the radical dose in each sample. HRF has a long track record of success for epitope mapping projects, even for conformational antibodies and highly complex proteins.
HRF can be used to map both linear and conformational epitopes at amino-acid resolution, even for complex, membrane proteins. By contrast, peptide mapping can only determine linear epitopes only and with much lower resolution- peptide level. HDX also
primarily provides peptide level epitope data and the back-exchange of deuterium can lead to challenges with data reproducibility. X-ray crystallography and Cryo-EM can be time-consuming (typically 6-12 months), expensive, and requires large quantities of correctly folded and natively processed target protein. A full epitope mapping project with HRF can be completed in under 2 weeks with a few hundred µg of protein without the need for protein purification or high cell surface expression.
High-resolution epitope and paratope data enables
PLIMB generates the radicals in sub-microsecond timescales which is faster than proteins can unfold. This ensures labeling of the native state of the protein and allows investigations of fast processes such as protein folding and weak protein-protein interactions. For every protein, we optimize the radical dose and monitor the dose dependency to ensure there are no structural perturbations. The instrument is equipped with a built-in cooling system that holds the protein samples at a constant temperature (typically 20 C) to prevent any heating due to the plasma.
At the completion of each project, Immuto will deliver a detailed project report as well as an in-person or virtual presentation of the final results. The report includes detailed information of the project including a graphical representation of the data, identities of the critical interacting residues, and a structural representation of the epitope mapped on the target protein. The report also includes detailed information of the experimental conditions, workflows, reagents, methods and data analysis protocols. As part of the project, Immuto’s highly experienced team can provide expert advice and guidance on discovery workflows including target identification, screening, lead optimization and formulation, as well as patent and regulatory filings.
HRF is suited to mapping antibody epitopes on any protein target, including GPCRs, ion channels, and proteins with complex folds, such as immuno-oncology targets.
We provide the fastest turnaround times in the industry. With our expedited service, projects can be delivered in under two weeks. The turnaround time for our standard service is typically four to six weeks
To begin an epitope mapping project, we require the sequence of the target protein and 500 µg of the antibody and antigen protein.
Developed in 2002, Hydroxyl Radical Protein Footprinting (HRF) has a long track record of success in academic labs for protein structural studies. At Immuto Scientific, we are leveraging this powerful, highly validated technique to analyze protein-protein interactions and map epitopes with an unprecedented degree of speed, resolution and accuracy.
“The service provided by Immuto was exceptional.
The sample prep optimization and analysis from
Immuto was high quality and the final project report
clearly explained the study design and
experimental outcomes."
Leveraging breakthrough technologies to map linear, conformational and discontinuous epitopes with amino acid level resolution
A revolutionary technology that generates free radicals from a
plasma for Protein Footprinting. PLIMB is used for analyzing
protein structure and interactions with unprecedented degree of
speed, resolution and accuracy.
High Resolution Epitope Mapping
Antibody Aggregation Analysis
Epitope-Based Screening
Epitope Target Identification
High Resolution Epitope Mapping
Antibody Aggregation Analysis
Epitope-Based Screening
Epitope Target Identification
PLIMB is a revolutionary technique that provides high resolution data on the native, in-solution structure of the therapeutic and target antigen in a rapid analysis that is applicable to a wide range of proteins.
Immuto utilizes a mass spectrometry-based protein footprinting technique called Hydroxyl Radical Footprinting (HRF)- a powerful, validated method for studying protein structure, dynamics and interactions. For HRF, side chain residues of proteins in solution are labeled with hydroxyl (OH) radicals. The labeled regions are localized and quantified using mass spectrometry. For epitope mapping, the labeling of an antibody bound vs unbound samples are compared to identify the epitope and paratope regions. At Immuto, we use our proprietary Plasma Induced Modification of Biomolecules (PLIMB) technology for HRF studies. The instrument generates controlled doses of radicals from an atmospheric-pressure plasma to irreversibly label the solvent-accessible regions of proteins in solution. PLIMB is a fully automated, high throughput HRF system that can label samples in a 96-well plate. The instrument has an integrated radical detection and feedback system to precisely control the radical dose in each sample. HRF has a long track record of success for epitope mapping projects, even for conformational antibodies and highly complex proteins.
HRF can be used to map both linear and conformational epitopes at amino-acid resolution, even for complex, membrane proteins. By contrast, peptide mapping can only determine linear epitopes only and with much lower resolution- peptide level. HDX also
primarily provides peptide level epitope data and the back-exchange of deuterium can lead to challenges with data reproducibility. X-ray crystallography and Cryo-EM can be time-consuming (typically 6-12 months), expensive, and requires large quantities of correctly folded and natively processed target protein. A full epitope mapping project with HRF can be completed in under 2 weeks with a few hundred µg of protein without the need for protein purification or high cell surface expression.
High-resolution epitope and paratope data enables
PLIMB generates the radicals in sub-microsecond timescales which is faster than proteins can unfold. This ensures labeling of the native state of the protein and allows investigations of fast processes such as protein folding and weak protein-protein interactions. For every protein, we optimize the radical dose and monitor the dose dependency to ensure there are no structural perturbations. The instrument is equipped with a built-in cooling system that holds the protein samples at a constant temperature (typically 20 C) to prevent any heating due to the plasma.
At the completion of each project, Immuto will deliver a detailed project report as well as an in-person or virtual presentation of the final results. The report includes detailed information of the project including a graphical representation of the data, identities of the critical interacting residues, and a structural representation of the epitope mapped on the target protein. The report also includes detailed information of the experimental conditions, workflows, reagents, methods and data analysis protocols. As part of the project, Immuto’s highly experienced team can provide expert advice and guidance on discovery workflows including target identification, screening, lead optimization and formulation, as well as patent and regulatory filings.
HRF is suited to mapping antibody epitopes on any protein target, including GPCRs, ion channels, and proteins with complex folds, such as immuno-oncology targets.
We provide the fastest turnaround times in the industry. With our expedited service, projects can be delivered in under two weeks. The turnaround time for our standard service is typically four to six weeks
To begin an epitope mapping project, we require the sequence of the target protein and 500 µg of the antibody and antigen protein.
Developed in 2002, Hydroxyl Radical Protein Footprinting (HRF) has a long track record of success in academic labs for protein structural studies. At Immuto Scientific, we are leveraging this powerful, highly validated technique to analyze protein-protein interactions and map epitopes with an unprecedented degree of speed, resolution and accuracy.
The service provided by Immuto was exceptional.
The sample prep optimization and analysis from
Immuto was high quality and the final project report
clearly explained the study design and
experimental outcomes.
-Senior Scientist at a top 5 US-based
pharmaceutical company
We are leveraging breakthrough technologies to transform drug discovery.
Acquiring detailed knowledge of epitope interactions is critical in the lead validation stage of drug discovery, as it provides insight into the binding mechanism, enabling the optimization of various properties of a drug candidate such as specificity and binding affinity.
Furthermore, a detailed epitope map can provide stronger intellectual property (IP) protection. Epitope claims included in drug patents protect against binders to a specific epitope of the given target, allowing for much broader IP protection.
PLIMB is a revolutionary technique that provides high resolution data on the native, in-solution structure of the therapeutic and target antigen in a rapid analysis that is applicable to a wide range of proteins.
Acquiring detailed knowledge of epitope interactions is critical in the lead validation stage of drug discovery, as it provides insight into the binding mechanism, enabling the optimization of various properties of a drug candidate such as specificity and binding affinity.
Furthermore, a detailed epitope map can provide stronger intellectual property (IP) protection. Epitope claims included in drug patents protect against binders to a specific epitope of the given target, allowing for much broader IP protection.
PLIMB is a revolutionary technique that provides high resolution data on the native, in-solution structure of the therapeutic and target antigen in a rapid analysis that is applicable to a wide range of proteins.