Ichthyophthirius multifiliis (also known as Ich, White Spot Disease, or Ichthy) is a common protozoan parasite that infects the skin and gills of freshwater and marine fish. It is a ciliated protozoan and is found worldwide in aquariums, ponds, and natural water sources. The parasite attaches to the skin of its host and feeds on the host’s blood and mucus. The antigen produced by Ich is known as Ichthyophthirius multifiliis antigen (Ich Ag). This antigen is a glycoprotein that has been used in immunological studies to detect the presence of Ich in fish. Ich Ag is also used to diagnose Ich infections in fish and to monitor the effectiveness of treatments. Ich Ag is also used in aquaculture to select fish that are naturally resistant to Ich infection.

Ichthyophthirius multifiliis cDNA and recombinant antigen can be used in a variety of applications. For instance, they can be used to develop diagnostic tests for fish parasites and to develop vaccines against fish parasites. Additionally, the cDNA and recombinant antigen can be used to study the molecular biology of Ichthyophthirius multifiliis and to develop new therapeutic strategies to treat the disease. Finally, they can be used as a research tool to identify novel targets for drug discovery and to develop animal models for studying the pathogenesis of Ichthyophthirius multifiliis.

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.