The mature cathepsin D was expressed in E.coli host strains BL21-CodonPlus (DE3) RP. Insoluble inclusion bodies were solubilized and part of the refolded protein was enzymatically active with the correct molecular weight of cathepsin D. The activity of the enzyme was determined using the fluorescence substrate FITC-hemoglobin. The purified mouse monoclonal antibodies against cathepsin D from the hybridoma cell line D101 were prepared.
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