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Cat# | Product Name | Swiss Prot# | Size | Price (US$) | Order |
PN1202 | Recombinant Protein-Monkeypox virus Cell surface-binding protein (a.a.31 to 304) | Q8V4Y0 | 100 µg | 1195 | |
PN1203 | Recombinant Protein-Monkeypox virus IMV heparin binding surface protein (a.a.31 to 324) | Q5IXT2 | 100 µg | 1195 | |
PN1204 | Recombinant Protein-Monkeypox virus P43-50 protein (a.a.21 to 204) | Q911W9 | 100 µg | 1195 | |
RPN1202 | cDNA-Monkeypox virus Cell surface-binding protein (a.a.31 to 304) | Q8V4Y0 | 2 µg | 1365 | |
RPN1203 | cDNA-Monkeypox virus IMV heparin binding surface protein (a.a.31 to 324) | Q5IXT2 | 2 µg | 1465 | |
RPN1204 | cDNA-Monkeypox virus P43-50 protein (a.a.21 to 204) | Q911W9 | 2 µg | 915 |
Monkeypox virus cDNA and recombinant antigen
Monkeypox virus is a double-stranded DNA virus that belongs to the genus Orthopoxvirus, which also includes the virus that causes smallpox. It is known to cause a disease in humans that is like but less severe than smallpox. The virus encodes several proteins, including a cell surface-binding protein, an IMV heparin binding surface protein, and a P43-50 protein.
The cell surface-binding protein is involved in binding the virus to host cells and is essential for viral entry and infection. The IMV heparin binding surface protein is involved in the formation of the virus particle and is important for its stability and infectivity. The P43-50 protein is involved in the assembly and packaging of the virus genome and is critical for viral replication and spread.
Studies of these proteins and their roles in the virus life cycle have provided important insights into the molecular mechanisms of monkeypox virus infection and have potential implications for the development of treatments and vaccines for this and other related viruses.
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.
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