Babesia microti is a tick-borne parasite that infects humans, causing babesiosis. The disease is characterized by fever, chills, sweats, headache, and fatigue, and can be severe in people with compromised immune systems. Babesia microti is transmitted by the blacklegged tick (Ixodes scapularis) and is endemic to certain regions of the United States.

Maltese cross form-related antigen is a key antigen of Babesia microti that is involved in the formation of the characteristic “Maltese cross” shape of the parasite in infected red blood cells. It is a potential target for the development of diagnostic tests and vaccines.

Seroreactive antigen 5-1-1 is another important antigen of Babesia microti that is involved in the pathogenesis of the disease. It is a potential target for the development of diagnostic tests and vaccines.

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 microti 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 functions and interactions of the key antigens associated with Babesia microti is crucial for the development of effective diagnostic tests and vaccines to prevent and control the spread of babesiosis in humans.

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.