Babesia odocoilei is a tick-borne parasite that infects deer, causing babesiosis. The disease is characterized by fever, anemia, and other nonspecific symptoms, and can be severe in some cases. Babesia odocoilei is transmitted by the blacklegged tick (Ixodes scapularis) and is endemic to certain regions of the United States.

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 odocoilei 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 odocoilei is crucial for the development of effective diagnostic tests and vaccines to prevent and control the spread of babesiosis in deer.

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.