Abstract: Different isolates of the soil bacterium Bacillus thuringiensis produce multiple crystal (Cry) proteins toxic. Due to these characteristics, genes encoding several Cry toxins have been engineered in order to be expressed by a variety of crop plants to control insectpests. A cry1Ea-type gene, designated cry1Ea8, was cloned from the strain Bt HZM2, through the recombinant DNA technology. Nucleotide sequencing for the cry1Ea8 gene is 99.49%~99.74% identical to the known cry1Ea gene. Homology comparison revealed that the deduced amino acid sequence of Cry1Ea8 had an identity over 99% with those of the known cry1Ea proteins. Domain Analysis showed that there were three domains in Cry1Ea8. N-terminal spiral domain was responsible for membrane insertion and pore-forming of the toxin and the other two domains was relevant to the receptor binding. It provided new selection for development of novel Bt products based on its toxins.