New York – Jan 25th, 2019 – Creative Biomart, a leading provider focuses on offering high-quality protein products and efficient protein manufacturing techniques, recently released protein interaction service which will support scientists to promote research, manufacturing and clinical development of native and recombinant proteins. The protein interaction service offered by Creative Biomart is featured with various analysis methods to offer comprehensive back-up, such as Yeast two-hybrid, Phage display technology, Fluorescence resonance energy transfer etc.
At present, defining protein and ribonucleoprotein complexes is critical for almost all aspects of cell biology because many cellular processes are regulated by stable protein complexes and their identification often provides insight into their function. The technology platform we offered can also be applied to study disease-associated proteins and ribonucleoprotein complexes to fully understand the molecular mechanisms of disease.
The protein interaction services in Creative Biomart involve the characterization of protein and ribonucleoprotein complexes by expression of bait proteins in mammalian cells. These baits are used as tools for isolating cellular proteins and their naturally interacting proteins or ribonucleoprotein complexes. They were isolated by affinity tag purification followed by identification of the interaction partner by mass spectrometry, immunoprecipitation and Western blot analysis. After isolation and identification of protein complexes, functional analysis allows scientists to obtain more information about the function of protein complex cells.
Common methods that are available to analyze the various types of protein interactions now can be found at Creative Biomart:
Co-immunoprecipitation (co-IP) is a popular technique for protein interaction discovery which is performed in substantially the same manner as immunoprecipitation (IP) of a single protein except that the antibody-precipitated target protein was used to coprecipitate the binding partner/protein complex. Basically, the interacting protein binds to the target antigen, and the target antigen binds to the antibody immobilized on the carrier. Immunoprecipitated proteins and their binding partners are typically detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Western blot analysis.
The pulldown analysis is similar in methodology to the co-immunoprecipitation as they both take the beaded support to purify the interacting proteins. However, the difference between the two methods is that although co-IP uses antibody capture protein complexes, the pull down assay uses a “bait” protein to purify any protein in the lysate that binds to the bait. Pull-down analysis is ideal for studying strong or stable interactions or those without antibodies available for co-immunoprecipitation.
Far-western blot analysis is different from western blot analysis which is just like pull-down assays differ from co-IP in the detection of protein-protein interactions by using tagged proteins instead of antibodies. Because protein-protein interactions are detected by incubation electrophoresis, respectively, have purified, labeled bait proteins rather than target protein-specific antibodies.
About Creative Biomart
Founded in 2005, Creative Biomart is dedicated to offering scientists and researchers with high quality protein products and services to greatly enhance the protein-related experiment performance and promote the development of protein studies. Creative Biomart is a well-recognized industry leader with highly-customized solutions to serve worldwide customers.
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