As a leader specialized in protein interaction analysis, Creative BioMart has acquired much experience and expert knowledge in protein interaction study. Whether you work in basic, pharmaceutical, cosmetic or agro-biotech research, we provide you with cutting-edge techniques to study protein interaction. Our customer-dedicated organization allows our passionate scientists to share scientific expertise with thousands of customers all over the world.
Yeast two-hybrid: Genome-wide screening of protein interactions by co-expression of bait with protein libraries.
Membrane-based yeast two-hybrid: Based on the split-ubiquitin protein complementation assay and detects protein interactions directly at the membrane.
Mammalian two-hybrid: Allows rapid and convenient analysis of protein-protein interactions in transfected mammalian cells.
Phage display technology: Obtain optimal protein binding by immobilization of an antigen on magnetic beads, and screening against a phage display library.
Surface plasmon resonance (SPR): The versatile label-free BIACORE technique allows detecting and monitoring of interactions in real time.
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.
Co-Immunoprecipitation (CO-IP): In vivo technique that detects naturally formed protein complex.
Pull-downs: Confirm the existence of a protein-protein interaction predicted by other research techniques and identify previously unknown protein-protein interactions as an initial screening assay.
Bio-layer interferometry (BLI): Quantitative and qualitative characterization of biomolecule interactions.
CLIP-Seq technology: RNA-binding landscape mapping of interacting proteins or RNA modification sites on a genome-wide scale.
Fluorescence resonance energy transfer (FRET): Test the direct interaction in vitro of two candidate proteins, suitable for both wild type and mutant proteins.
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.
Far-western blotting: This method employs non-antibody proteins to probe the protein(s) of interest on the blot.
Protein binding site mapping: Locate the binding sites with a high degree of confidence and predict the druggability of those sites.
Benefits working with us:
We will be glad to discuss details of intended interaction studies with you and develop experimental strategies/methods tailored to your requirement. Please get in contact with Creative BioMart for more information or a detailed discussion.
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