Study on Method of Purification of GST-tagged Proteins from Inclusion Bodies

The aim was to study the method of purification of GST-tagged proteins from inclusion bodies.The vector PGEX-4T1-Rpfd expressed Rpfd-GST fusion protein was transformed into E.coli DH5a and protein expression was induced with IPTG.The effect of these factors is observed on the impact of protein purification by comparing lysis with guanidine hydrochloride and pretreatment with Novagen Protein Refolding Kit,and adjusting the different types of protein refolding solution.The active GST fusion protein can be efficiently purified,through removing soluble protein after ultrasonic treatment,and then using the reaction mixture containing 20 mmol Tris-HCl and 0.1 mmol DTT for rehabilitation.To remove soluble protein expression and change the formula of protein refolding solutions can effectively improve protein purification of GST-tagged proteins from inclusion bodies.