Hydroxyl Radical Footprinting (HRF) for characterizing aggregation
PLIMB for Aggregation: HRF resolves regions involved in protein aggregation, conformational changes, and intermediate structures that form during aggregation at amino acid-level resolution.
Furthermore, it delivers results in under a week and is compatible with a 96-well plate high throughput format to characterize and compare aggregation sites of a multitude of samples with different formulations, concentrations, or temperatures.
Approach: Hydroxyl radicals rapidly and covalently modify amino acid side chains of proteins.
Once the protein has undergone the rapid labeling process, the sample is enzymatically digested and analyzed according to well established proteomics techniques.
Other Services
Protein Small Molecule Interaction
Gain detailed insights into - ligand-protein interactions.
Pinpoint amino acid level hotspots to locate binding interactions.
Generate a detailed map of ligand-induced higher-order structural changes.
Protein-Protein Interaction
Map the specific regions of interactions between proteins.
Characterize drug/receptor interactions, protein aggregation, or dimerization.
Protein Higher Order Structure
Characterize and detect subtle differences in protein higher order structure (HOS).
Use HOS for measuring comparability studies for characterizing biosimilar-innovator differences, expression platforms, formulation, or changes based on buffer or environmental conditions.
More Information:
Thank you. The file will open in a new window
Oops! Something went wrong while submitting the form.
Thank you. The file will open in a new window
Oops! Something went wrong while submitting the form.
Thank you. The file will open in a new window
Oops! Something went wrong while submitting the form.
hank you. The file will open in a new window
Oops! Something went wrong while submitting the form.
Hydroxyl Radical Footprinting (HRF) for characterizing aggregation
PLIMB for Aggregation: HRF resolves regions involved in protein aggregation, conformational changes, and intermediate structures that form during aggregation at amino acid-level resolution.
Furthermore, it delivers results in under a week and is compatible with a 96-well plate high throughput format to characterize and compare aggregation sites of a multitude of samples with different formulations, concentrations, or temperatures.
Approach: Hydroxyl radicals rapidly and covalently modify amino acid side chains of proteins.
Once the protein has undergone the rapid labeling process, the sample is enzymatically digested and analyzed according to well established proteomics techniques.