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Author Topic:   Yeast two hybrid 
posted 12-21-2015 09:22 AM     Click Here to See the Profile for ClairHall     Edit/Delete Message Reply w/Quote
As a leader specialized in protein interaction analysis, Creative BioMart has acquired long 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 services to study protein interaction. Our customer-dedicated organization allow our passionate scientists to share scientific expertise with thousands of customers all over the world.
Yeast two-hybrid: Co-expression of proteins for the determination and characterization of protein interactions is achieved with Yeast Two-Hybrid technology.

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.

Far-western Blotting: This method employs non-antibody proteins to probe the protein(s) of interest on the blot. In this way, binding partners of the probe (or the blotted) protein may be identified. Multiple approaches can be used to detect far-Western blot protein-protein interactions depending on the presence of a radiolabel or affinity tag on the bait protein.
More at http://www.creativebiomart.net/Protein-Interaction.htm


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