Proteins rarely function alone, and many molecular processes in cells are coordinated by protein complexes or protein networks composed of proteins. Many processes in these complex networks (such as replication and expression of genetic information, substance metabolism, etc.) are related to protein-protein interactions. Abnormal protein-protein interactions are associated with a variety of diseases. Therefore, studying protein interactions can help to understand related diseases and can discover protein targets.
Identification of insect-interacting proteins by mass spectrometry is the identification of insect-interacting proteins by mass spectrometry. Lifeasible provides identification services of interacting proteins in insects based on mass spectrometry obtain a range of proteins that interact with the target protein in insects.
Protein solution main sources | Detail |
IP | The classical method for studying protein interactions based on the specificity of the interaction between antibody and antigen is an effective method for determining the physiological interaction of two proteins within an intact cell and is one of the most widely used methods for antigen detection and purification. |
Co-IP | A common technique for studying protein-protein interactions, often used to determine whether two known proteins can bind in a cell to produce an interaction, and for identifying unknown proteins that interact with a particular protein. |
Pull-down | In vitro assays for protein-protein interactions are used to verify the interaction of two known proteins or to screen for unknown proteins that interact with known proteins. |
Lifeasible uses mass spectrometry to identify insect intercalating proteins, mainly for the identification of interacting proteins, prior to which the intercalating proteins need to be screened and isolated by protein intercalation assays. Most of the samples used in mass spectrometry for the identification of reciprocal proteins are derived from IP, Co-IP protein interactions, pull-down protein samples, tandem affinity purification techniques or protein microarrays.
The advantages of the Co-IP technique are that it can isolate the interacting protein complexes in their natural state, but the disadvantage is that it is less sensitive and cannot be used for low affinity and instantaneous protein interaction analysis; the advantage of the pull-down technique is that it can directly detect protein interactions without the interference of other intracellular conditions. The disadvantage is that it needs to be performed outside the cell and does not accurately reflect the protein interaction relationships within the cell. With regard to protein interaction analysis, researchers can choose different methods to perform according to your needs.
Fig 1. Service flow for the identification of interacting insect proteins by mass spectrometry.
Lifeasible offers services for the identification of insect intercalating proteins. We use LC-ESI-MS/ MS protein identification techniques to identify proteins in purified solution samples such as IP, Co-IP, pull-down, etc., to obtain a range of proteins that interact with the target protein in insects. If you are interested in our services or if you have any questions, please click online inquiry for more detailed information.