Optimal Purification Condition and Identification of GST-Aβ_(42)Expression in Escherichia Coli

Objective:To improve the expression ofβ-amyloid peptide in Escherichia coli,and also to lay a foundation for further study on its Mechanism and vaccine function.Method:The results indicated that the soluble expression level of GST-Aβ_(42) fusion protein could be promoted when cells were cultured for 4 h at 37℃,and then shifted to 25℃for 2 h to induce the expression of GST-Aβ_(42) with 1 mmol/L IPTG as final concentration.The expression product was determined by SDS-PAGE and Western Blotting analysis.Result: SDS-PAGE analysis result showed that the molecular mass of GST-Aβ_(42) fusion protein was about 32 kD as expected,and Western Blot- ting analysis indicated that both anti-Aβ_(42) and anti-GST antibody could react specifically against the fusion protein.Conclusion:The opti- mized expression of GST-Aβ_(42) will be useful for future research on the mechanism of Aβ_(42) on Alzheimer's Disease and provide sufficient foundation for the further study on Aβ_(42) vaccine.