KMD Bioscience has been dedicated to protein-protein interaction research for many years. Protein-protein interactions reveal the interaction patterns between molecules, playing a crucial role in the study of protein structure and function. With rich experience in recombinant tag protein expression, we can express recombinant proteins with GST, Myc-tag, Flag-tag, HA-tag, and other tags in both prokaryotic and eukaryotic expression systems. Additionally, we have advanced detection equipment and mature technologies, with its immunoprecipitation and Pull-Down techniques originating from the IPS laboratory at Kyoto University, Japan, ensuring the accuracy of experiments. We are committed to providing high-quality services and offers one-stop technical services, from Recombinant Protein Production to Pull-Down Protein-Protein Interaction Detection, to meet various customer needs.

The Pull-Down assay is a method used to detect molecular interactions under in vitro conditions. This technique can be used to verify protein-protein interactions or to screen for target proteins. Similar to immunoprecipitation, Pull-Down assays utilize protein-protein and protein-other biomolecule interactions to capture and study target molecules. The principle is that a tagged bait protein is specifically captured by a solid-phase affinity ligand that binds to the tag, with secondary "affinity supports" used to purify other proteins that interact with the bait protein. By performing SDS-PAGE electrophoresis analysis, or combining with Western Blot verification and LC-MS/MS, the purified eluted protein complexes can be further identified, revealing the proteins that interact with the bait protein.

We have established and perfected a series of immune-based detection technologies, including GST fusion protein pull-down, streptavidin-labeled pull-down, Co-IP, and ChIP-qPCR services. Among them, pull-down technology and streptavidin-labeled pull-down technology are used for protein and nucleic acid (RNA/DNA) researches.