posted 12-21-2015 09:22 AM         

Phage display technology: Obtain optimal protein binding by immobilization of an antigen on magnetic beads, and screening towards a phage library. Using magnetic separation technology, more positives are found and the amount of false positives is kept at a minimum.

Surface Plasmon Resonance (SPR): The versatile label-free BIACORE technique allows detecting and monitoring the interactions in real time. Kinetic rate constants (kon/koff), thermodynamics parameters and binding affinity can be determined as well.

Fluorescence Resonance Energy Transfer (FRET): Test the direct interaction in vitro of two candidate proteins, is applied to both wild type and mutant proteins. Full-length proteins or fragments, peptides, cytoplasmic or extracellular proteins, loops and tails of membrane proteins can all be tested. Please refer to at Creative BioMart if you need any proteins fluorescently labeled.

Protein Array: This technique is a high-throughput method used to track the interactions and activities of proteins, and determining function on a large scale. Its main advantage lies in the fact that large numbers of proteins can be tracked in parallel.

Co-Immunoprecipitation (CO-IP): Detect the naturally formed complex, capable of filtering the fake positives brought up by overly expressed target protein as well as interactions between modification dependent proteins.

Pull-downs: Confirm the existence of a protein-protein interaction predicted by other research techniques (e.g., CO-IP) and identify previously unknown protein-protein interactions as an initial screening assay. We offer different types of active Fusion tag pull-down and tag-based pull-down assays, including, Glutathione S-transferase (GST), Poly-histidine (polyHis or 6xHis), biotin, glutathione, metal chelate (Nickel or cobalt chelate complexes) and streptavidin.

Biomolecular fluorescence complementation (BiFC): This technique is based on the principle that two nonfluorescent fragments of a fluorescent protein dissected at appropriate site are brought together and reconstructed to fluorescence, depending on the association or interaction between the protein fused to each fragment.