Rickettsia heilongjiangensis is a bacterium that belongs to the spotted fever group of Rickettsia. It is mainly found in China and Russia and is transmitted to humans and animals through the bite of infected ticks. This bacterium is known to cause a severe form of spotted fever in humans, with symptoms that include fever, headache, rash, and muscle aches.

One of the key components of Rickettsia heilongjiangensis is its surface antigen. This is a protein that is located on the surface of the bacterium and plays an important role in the interaction between the bacterium and the host. The surface antigen of Rickettsia heilongjiangensis has been identified and studied extensively in recent years, and it is believed to be an important factor in the pathogenesis of the disease.

The surface antigen of Rickettsia heilongjiangensis is highly immunogenic, meaning that it can elicit an immune response in the host. This response is characterized by the production of antibodies that recognize and bind to the surface antigen. These antibodies can help to neutralize the bacterium and prevent it from causing disease.

Rickettsia heilongjiangensis antigen is a protein antigen found in the bacterium Rickettsia heilongjiangensis. This antigen is used to diagnose infections caused by this microorganism, as well as to study the genetic diversity of this bacterium. It can be detected in serum, cerebrospinal fluid, and tissue samples of patients with suspected rickettsial infection. The antigen has been used in the development of a rapid diagnostic test for the detection of R. heilongjiangensis.

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.