Polybia scutellaris rioplatensis is a species of wasp commonly found in the South American region. This species, like other social wasps, can cause painful stings that can be dangerous for some individuals. Moreover, the venom of Polybia scutellaris rioplatensis contains an allergenic protein known as Antigen 5, which can trigger allergic reactions in some people.

Antigen 5 is a glycoprotein antigen found in the venom of the species of wasp Polybia scutellaris rioplatensis. It is an immunomodulatory protein and has been used for therapeutic purposes. This antigen has been found to have anti-inflammatory and immunomodulatory effects in mice, as well as anti-tumor activity in vitro. It has been suggested that this antigen may have potential therapeutic applications in the treatment of autoimmune diseases, cancer, and other inflammatory diseases.

Polybia scutellaris rioplatensis cDNA and recombinant antigens can be used in the detection of anti-Polybia scutellaris rioplatensis antibodies. The cDNA can be used for the synthesis of Polybia scutellaris rioplatensis-specific antibodies, which can then be used to detect the presence of anti-Polybia scutellaris rioplatensis antibodies in a sample. The recombinant antigen can be used to detect the presence of anti-Polybia scutellaris rioplatensis antibodies in a sample using immunoassays such as ELISA and Western blotting. Both of these techniques are highly sensitive and specific for the detection of anti-Polybia scutellaris rioplatensis antibodies.

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.