The biotin labeled peptide contains a special functional region and an unmodified peptide equivalent to a reference, which can be anchored on avidin conjugated magnetic beads and incubated with the target sample (such as nuclear extract or purified recombinant protein). The unbound protein was removed by washing, and then the bound protein was eluted. SDS/ PAGE analysis could be observed directly by protein staining. By comparing the proteins that bind to modified and unmodified peptides respectively, it is possible to identify candidates, that is, "reader" proteins of specific functional proteins. Biotin labeled peptides with some special modifications can be chemically synthesized with a purity of more than 80%.
Application
Biotin labeled peptides can be used for protein purification, detection, curing, drug targeting, protein structure analysis and so on. The simplest way to detect a substance that interacts with a polypeptide is to use the peptide to do affinity pull-down experiments, and then directly detect the binding protein. Protein in vitro binding (Pull-down) test can be used to verify the existence of protein-protein interactions (predicted by other methods, such as immunoprecipitation) and as a primary screening test to identify unknown protein-protein interactions. By competitive blocking binding, synthetic peptides are often used to verify hypothetical protein-protein interactions.
Our Advantages
- A rapid and high flux platform for peptide synthesis
- Strict quality control: MS and HPLC identification results are provided for each peptide product
- Optimized Chemistries: Expertise in hundreds of cross linking modifications, activation and/or conjugation with reactive cross linkers with optimized labeling ratio
- Superior technical support: assist client from design to delivery
- Data analysis, detailed report with results and discussion
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