GST Pull-down to study protein-protein interactions (CAT#: STEM-MB-0164-WXH)

Introduction

The GST (Glutathione S transferase) pull-down has proven to be a powerful technique for studying protein-protein interactions, allowing the identification of unknown proteins that interact with known proteins and confirming suspected interactions, as well as identifying the presence of interactions between two known proteins.
Mechanistically, the probe protein is fused with GST by recombinant technology, and the fusion protein can then be bound to GTH (Glutathione) on the solid support through GST due to affinity attraction. Therefore, proteins that interact with fusion proteins when passing through the column or mixed with the solid phase complex are adsorbed and separated.

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Applications Procedure Notes

Applications

• Validation of the interaction of two known proteins.
• Screening for unknown proteins that interact with known proteins.

Procedure

1. Construction of prokaryotic expression vector with GST tag by recombinant technology;
2. Expression of the fusion protein with GST tag by prokaryotic expression system;
3. Obtaining high purity fusion protein via the GST affinity purification column and using the GST affinity purification column for protein-to-protein interaction detection;
4. Using WB and MS detection to verify the interaction between proteins or screen for target proteins.

Notes

Customers provide:
1. Probe gene and target gene-related sequence information
2. Species and types of samples

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