Babesia orientalis is a tick-borne parasite that infects cattle, causing babesiosis. The disease is characterized by fever, anemia, and other nonspecific symptoms, and can be severe in some cases. Babesia orientalis is transmitted by ticks of the genus Rhipicephalus and is endemic to certain regions of Asia.

Heat shock protein 70 (HSP70) is a chaperone protein that is involved in the folding and transport of proteins in the cell. It is also a key antigen of Babesia orientalis that is upregulated during the intraerythrocytic stage of the parasite’s life cycle. HSP70 is a potential target for the development of diagnostic tests and vaccines.

In conclusion, understanding the function and interaction of the key antigen associated with Babesia orientalis is crucial for the development of effective diagnostic tests and vaccines to prevent and control the spread of babesiosis in cattle.

The use of recombinant proteins/cDNA in academic research and therapeutic applications has skyrocketed. However, in heterologous expression systems, successful recombinant protein expression is dependent on a variety of factors, including codon preference, RNA secondary structure, and GC content. When compared to pre-optimization, more and more experimental results demonstrated that the expression level was dramatically increased, ranging from two to hundred times depending on the gene. Bioclone has created a proprietary technology platform that has resulted in the creation of over 6,000 artificially synthesized codon-optimized cDNA clones (cloned in E. coli expression Vector), which are ready for production of the recombinant proteins.