Alliance Protein Laboratories specializes in biophysical and biochemical characterization of proteins, nucleic acids, and other macromolecular assemblies (viral vectors for gene therapy, protein-polymer conjugates, etc.) We offer characterization services not available in-house from any other U.S. contract lab, including analytical ultracentrifugation (AUC) and concentration-gradient multi-angle light scattering (CG-MALS). Our scientists pioneered the application of a number of these biophysical techniques in the biotechnology industry.
A.P.L. offers various techniques to characterize or compare protein higher order structure (HOS). These include methods to characterize protein folding (secondary/tertiary structure), protein stability, protein conformation, protein aggregation, and the oligomeric state of the native protein (quaternary structure).
For characterization of oligomeric state and aggregation A.P.L. offers analytical ultracentrifugation (AUC), light scattering, and native gel electrophoresis analysis services. For characterization of protein conformation and stability we primarily use circular dichroism (CD), differential scanning calorimetry (DSC), and fluorescence, but native gels are also useful.
A.P.L. can also quantify protein-protein or protein-ligand interactions, e.g. for functional assessment of antibody-antigen or hormone-receptor pairs using analytical ultracentrifugation.
All the techniques offered and some of their uses are listed on the Methods Summary page. Several general applications and the benefits of detailed characterization are discussed on the Example Applications page. More details about the background and applications for some of the techniques are discussed on their individual pages:
Key Benefits from Using A.P.L. for Characterization Services
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