Plasmodium Chabaudi is a species of protozoan parasite that is commonly used in laboratory studies of malaria. This parasite primarily infects rodents, but it can also infect other animals, including primates.

Acidic Phosphoprotein, also known as 50 kDa antigen, is a protein that is produced by the Plasmodium Chabaudi parasite during the blood stage of its life cycle. This protein is believed to play a role in the invasion of the parasite into host red blood cells, as well as in the immune response of the host.

Apical Membrane Antigen 1 (AMA1) is another protein produced by the Plasmodium Chabaudi parasite. This protein is located on the surface of the parasite and is involved in the invasion of host red blood cells. AMA1 is also a key target for the development of vaccines against malaria.

Erythrocyte-binding-like Protein (EBL) is a family of proteins that are produced by the Plasmodium Chabaudi parasite. These proteins are involved in the invasion of the parasite into host red blood cells and are a key focus of research into the development of new treatments for malaria.

Understanding the role of Acidic Phosphoprotein, Apical Membrane Antigen 1, and Erythrocyte-binding-like Protein in Plasmodium Chabaudi is essential for the development of new treatments for malaria. By targeting these proteins, researchers hope to develop vaccines and drugs that can prevent the invasion of the parasite into host red blood cells, as well as treatments that can kill the parasite once it has invaded.

In addition, research into Plasmodium Chabaudi may have important implications for our understanding of the broader biology of malaria. By studying this parasite in detail, researchers may be able to develop new insights into the mechanisms of other malaria parasites, including those that affect humans.

Preparations of Plasmodium chabaudi cDNA and recombinant antigens can be used in a variety of applications. These preparations can be used for immunization studies to assess the efficacy of different vaccine candidates, as well as for diagnostic tests to detect Plasmodium infection. Plasmodium cDNA and recombinant antigens can also be used for the development of therapeutic agents, such as antibodies and small molecule inhibitors, to treat Plasmodium infections. In addition, these preparations can be used for the study of Plasmodium biology, such as understanding how the parasite infects a host, how it replicates and spreads, and how it evolves and adapts in different environments.

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.