Rickettsia canadensis is an obligate intracellular bacterium that belongs to the genus Rickettsia, family Rickettsiaceae. It is primarily transmitted to humans through the bite of an infected tick and can cause a disease known as Canadian tick-borne relapsing fever.

As you mentioned, Rickettsia canadensis expresses several cell surface antigens, including Sca1 and the 190-kDa antigen. These antigens are important virulence factors that play a significant role in the pathogenesis of the disease.

Sca1 (surface cell antigen 1) is a protein that is located on the outer membrane of Rickettsia canadensis. It is involved in the adhesion of the bacteria to host cells and is essential for invasion and replication within host cells. Sca1 is also known to be a major target for the host immune system during infection.

The 190-kDa antigen is another surface protein that is expressed by Rickettsia canadensis. It is a major immunodominant protein that is recognized by the host immune system during infection. The 190-kDa antigen is also involved in the adhesion and invasion of host cells by Rickettsia canadensis.

Application of Rickettsia canadensis cDNA and recombinant antigen in a variety of immunological assays. These assays can be used to detect the presence and levels of Rickettsia canadensis DNA, RNA, and proteins in samples. These assays can also be used to identify and measure the production of antibodies against the pathogen in individuals exposed to it. Additionally, the assays can be used to evaluate the effectiveness of vaccines and other treatments against Rickettsia canadensis infections.

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.