Mouse mammary tumor virus cDNA and Antigen

Mouse mammary tumor virus (MMTV) is a type of retrovirus that is known to cause mammary tumors in mice. The virus is composed of various proteins, including the p10 matrix protein, pp21 capsid protein, p27 capsid protein, p14 nucleocapsid protein, and a superantigen. The p10 matrix protein plays a role in virus assembly and budding, while the pp21 and p27 capsid proteins are involved in protecting the virus genome during its replication cycle. The p14 nucleocapsid protein is responsible for packaging the viral RNA genome into new virus particles. The superantigen produced by MMTV is believed to play a role in the development of mammary tumors by inducing a strong immune response that promotes inflammation and tissue damage.
Mouse mammary tumor virus (MMTV) is a retrovirus that can induce breast cancer in mice. It is a type B retrovirus that has a single-stranded RNA genome. The virus has several proteins that are important for its replication and pathogenesis.

One of the major proteins of MMTV is the matrix protein p10 MA. This protein plays a role in viral assembly and budding from infected cells. Another important protein is pp21 XX, which is the viral capsid protein. It is responsible for protecting the viral genome and aiding in its transport into host cells.

The virus also contains p27 CA, which is the core protein of the virion. This protein is essential for the formation of the virion and its infectivity. Another protein, p14 NC, is the nucleocapsid protein that encapsidates the viral genome.

In addition to these structural proteins, MMTV also encodes a superantigen that is involved in immune system modulation. This superantigen can activate large numbers of T cells, leading to a strong inflammatory response.

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.