Scomber japonicus, also known as the chub mackerel, is a popular fish species found in the Pacific and Indian Oceans. With its rich flavor and high nutritional value, it is a favorite among seafood lovers. However, there is much more to this fish than just its taste. In recent years, researchers have been exploring the biology of Scomber japonicus and the various proteins and enzymes that play a vital role in its survival.

One such protein is Endoplasmic Reticulum Lumenal L-Amino Acid Oxidase (ERAO), an enzyme that is involved in the metabolism of amino acids. In this article, we will delve deeper into the world of Scomber japonicus and ERAO, exploring their significance and impact.

What is Endoplasmic Reticulum Lumenal L-Amino Acid Oxidase (ERAO)?
ERAO is an enzyme involved in the metabolism of amino acids. It is found in the endoplasmic reticulum of cells.

Scomber japonicus cDNA and recombinant antigen can be used to develop an immunoassay. The development of an immunoassay requires the identification of target proteins in the fish species of interest. Once identified, these proteins can be cloned and expressed as recombinant proteins. The recombinant proteins can then be used to produce monoclonal or polyclonal antibodies. These antibodies can then be used to detect specific antigens in the species of interest. Additionally, the cDNA of the species of interest can be used to develop a PCR-based assay to detect specific genes or proteins. These assays can then be used to identify and quantify specific proteins in the species of interest.

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.