Viral Co-IP/MS Analysis Service

Protein co-immunoprecipitation (co-IP) is a popular technique that is commonly used to identify physiologically relevant protein-protein interactions. The method is based on the ability of targeted protein-specific antibodies to stabilize and specifically bind to complexes containing bait proteins. Studies have shown that co-IP with optimized workflows can preserve the structural integrity of its associated protein complexes and biologically important protein conformations, such as post-translational modifications (PTMs). By coupling high-resolution mass spectrometry (MS), co-IP serves as a high-throughput method to identify multiple virus-host interactions.

Creative Proteomics is a forward-looking research institute as well as a leading custom service provider in the field of viral proteomics. We provide custom experimental design and detailed research reports according to customers' specific project needs. Here, we can perform the Co-IP technique coupled with LC-MS/MS and bioinformatics analysis to screen and analyze virus-host protein interactions, promoting the investigations of viral proteomes and host responses associated with viral infections.

How does Co-IP/MS work?

In a common Co-IP/MS experiment, samples are lysed under non-denaturing conditions to avoid the interruption of protein interactions during the extraction process. In order to isolate the virus-host complexes in solutions of host tissue homogenate, the antibodies are usually immobilized with agarose or magnetic beads. When the target protein is immunoprecipitated with specific antibodies, interacting partners of this protein may also precipitate. Then repeated washing is conducted to remove non-specifically bound proteins. Co-immunoprecipitated interacting partners are eluted, separated, digested in-gel, and finally identified by tandem MS (MS/MS).

Characteristics of Co-IP/MS method

• Remain the structural integrity and biologically important protein conformations, such as PTMs.
• Study protein interactions in their natural state.
• Analyze interacting proteins in a fast, high throughput, and comprehensive manner.

Service offering in Creative Proteomics

Based on skillful scientists, powerful mass spectrometry platforms, and optimized workflows, we have launched a protein interaction analysis service package using the Co-IP/MS method. Customers only need to tell us the purpose of their projects, we will be responsible for all subsequent matters of the experiments. Our specific services include cell culture, virus infection, protein isolation and purification, protein co-IP, LC-MS/MS analysis, MS data, and bioinformatics analysis. It is worth noting that, if necessary, we will use stable isotope-labeling method (such as stable isotope labeling of amino acids in cell culture, SILAC) to label the samples prior to the performance of the Co-IP experiment, to meet the need for high-throughput quantitative analysis of protein-protein interaction (PPI) networks in specific situations.

Workflow of our Co-IP/MS experiment

Virus-host protein interactions are essential for viral propagation and movement, as viruses' life cycles are largely dependent on the protein synthesis machinery of host cells. Therefore, the identification of virus-host protein interaction networks is one of the critical steps in understanding how pathogens cause disease. Co-IP/MS provides a high-throughput way to characterize virus-host interactomes in a single experiment. Simply let us know about your research needs and we will respond rapidly to your inquiry.Contact us right now!

Reference

1. DeBlasio, S. L., et al. (2017). "Evaluation of a bead-free coimmunoprecipitation technique for identification of virus–host protein interactions using high-resolution mass spectrometry." Journal of biomolecular techniques: JBT, 28(3), 111.

* For research use only.