The study of biomolecular interaction is of great significance for clarifying the mechanism of biological reaction and for revealing the essence of life phenomena. Biomolecular interaction includes the interactions between protein and protein, protein and nucleic acid, protein and ligand, nucleic acid and ligand, and other interactions. Commonly used research technologies for studying biomolecular interaction include biophysics, biochemistry and computational biology. In drug discovery research, these technologies are often used to study the interaction between drug molecules and biological targets (usually protein targets). These studies play an important role for clarifying the mechanism of drug action and for optimizing the properties of drug leads. Our biomolecular interaction services include a variety of biophysical technologies, such as ASMS, SPR, HDX-MS, Native-MS, Intact-MS, TSA, X-ray crystal structure analysis of protein, cryo-EM single particle analysis and microcrystal electron diffraction (MicroED) . These biomolecular interaction services can meet the research needs of customers for different projects, such as ASMS, antibody/antigen interactions, interactions between small molecule drugs and target proteins, E3 ligase-PROTAC-target protein ternary system interactions, and studies on the mechanism of protein-protein interaction.
We support E. coli, baculovirus/insect cell (Sf9/Hi5/Sf21/S2), and mammalian (HEK293/CHO transient and stable) platforms, as well as Pichia pastoris for select targets. In general, selection depends on the target class:
We routinely advise on system choice based on target biology, downstream application (crystallography vs. cryo-EM vs. SPR vs. in vivo), and timeline.
| Protein Type | Recommended System |
| Cytosolic proteins (Small) | E. coli |
| Cytosolic proteins (Large) | Insect/Mammalian |
| Enzymes | E. coli /Insect |
| Kinases | E. coli/Insect |
| GPCRs | Insect/Mammalian |
| Antibodies | Mammalian |
| Secreted proteins | Mammalian |
| Membrane proteins | Insect/Mammalian |
| Multi-protein complexes | Insect/Mammalian |
We support E. coli, baculovirus/insect cell (Sf9/Hi5/Sf21/S2), and mammalian (HEK293/CHO transient and stable) platforms, as well as Pichia pastoris for select targets. In general, selection depends on the target class:
We routinely advise on system choice based on target biology, downstream application (crystallography vs. cryo-EM vs. SPR vs. in vivo), and timeline.
| Protein Type | Recommended System |
| Cytosolic proteins (Small) | E. coli |
| Cytosolic proteins (Large) | Insect/Mammalian |
| Enzymes | E. coli /Insect |
| Kinases | E. coli/Insect |
| GPCRs | Insect/Mammalian |
| Antibodies | Mammalian |
| Secreted proteins | Mammalian |
| Membrane proteins | Insect/Mammalian |
| Multi-protein complexes | Insect/Mammalian |