Brugia pahangi is a filarial nematode that causes lymphatic filariasis in animals, particularly in dogs and cats. The infection can cause severe damage to the lymphatic system and result in significant morbidity and mortality in infected animals.

Cuticular glycoprotein gp29 is a key antigen associated with Brugiapahangi. This antigen is expressed on the surface of the nematode and plays an important role in its survival and infectivity. Cuticular glycoprotein gp29 has been identified as a potential target for the development of diagnostic tests and vaccines for lymphatic filariasis caused by Brugiapahangi.

Understanding the function and interaction of the key antigen, cuticular glycoprotein gp29, is crucial for the development of effective diagnostic tests and vaccines to prevent and control the spread of lymphatic filariasis caused by Brugia pahangi in animals.

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.