Bio-Rad Laboratories has announced that the Proteon XPR36 protein interaction array system has been included in two comparison studies authored by Pfizer scientists.
The first study, entitled 'Determining Kinetics and Affinities of Protein Interactions Using a Parallel Real-Time Label-Free Biosensor, the Octet', was published in Elsevier's Analytical Biochemistry Journal in June 2008.
In the study, researchers compare the Proteon XPR36 system with several other biosensors to detect and quantify molecular interactions.
The researchers used a monoclonal antibody against a panel of peptides to compare the three sensors.
The Proteon XPR36 system was determined to provide high-quality data in a more multiplexed format.
In addition, results of the experiments provide a benchmark for assessing the performance of the various sensors.
The second study, entitled 'Probing the Binding Mechanism and Affinity of Tanezumab, a Recombinant Humanised Anti-NGF monoclonal Antibody, Using a Repertoire of Biosensors', was published in Protein Science in August 2008.
It describes the use of four complementary biosensors to characterise the kinetics of human nerve growth factor (NGF) binding to a humanised NGF-neutralising monoclonal antibody.
This interaction was found to be difficult to study since NGF is an obligate homodimer, various assay orientations and immobilisation methods were used to minimise avidity, while keeping NGF in as native a state as possible.
Researchers found that the Proteon XPR36 system allowed for multiple analyte concentrations as well as multiple ligands to be addressed simultaneously and revealed the effect of five different immobilisation methods on NGF.
