Babesia equi, also known as Theileriaequi, is a tick-borne parasitic protozoan that infects horses and other equids, causing a disease known as equine piroplasmosis. The disease is characterized by fever, anemia, jaundice, and hemoglobinuria, and can be fatal if left untreated. Babesia equi is transmitted by ticks of the genus Rhipicephalus and can also be transmitted by blood transfusion or contaminated needles.

Erythrocyte merozoite antigen 1 (EMA1) is a key antigen of Babesia equi that plays a critical role in the invasion of host red blood cells. It is a surface protein that is highly conserved among different strains of Babesia equi and is a potential target for the development of vaccines and diagnostic tests.

Merozoite antigen 2 and 3 (MA2 and MA3) are other important antigens of Babesia equi that are involved in the invasion of red blood cells. MA2 is a surface protein that binds to host cell receptors, while MA3 is a secreted protein that promotes the survival of the parasite within the host.

Equi merozoite antigen 1 (EMA1), also known as Babesia equi merozoite surface antigen 1 (BEMSA1), is a surface protein that is closely related to EMA1. It is also involved in the invasion of red blood cells and is a potential target for vaccines and diagnostic tests.

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 equi that is upregulated during the intraerythrocytic stage of the parasite’s life cycle. HSP70 is a potential target for the development of vaccines and diagnostic tests.

Ms1-2 protein and Ms1-3 protein are two other important antigens of Babesia equi that are involved in the invasion of red blood cells. Ms1-2 is a secreted protein that binds to host cell receptors, while Ms1-3 is a surface protein that is involved in the formation of a complex with other parasite proteins.

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.