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Cat# | Product Name | Swiss Prot# | Size | Price (US$) | Order |
PN1138 | Recombinant Protein-Mmarburgvirus Membrane-associated protein VP24 (a.a.21 to 253) | Q1PD62 | 100 µg | 1195 | |
PN1139 | Recombinant Protein-Mmarburgvirus VP30 (a.a.21 to 281) | Q1PD56 | 100 µg | 1195 | |
PN1140 | Recombinant Protein-Mmarburgvirus Polymerase cofactor VP35 (a.a.31 to 329) | Q1PD52 | 100 µg | 1195 | |
PN1141 | Recombinant Protein-Mmarburgvirus Matrix protein VP40 (a.a.31 to 303) | Q1PD51 | 100 µg | 1195 | |
RPN1138 | cDNA-Mmarburgvirus Membrane-associated protein VP24 (a.a.21 to 253) – 2 µg | Q1PD62 | 2 µg | 1160 | |
RPN1139 | cDNA-Mmarburgvirus VP30 (a.a.21 to 281) | Q1PD56 | 2 µg | 1300 | |
RPN1140 | cDNA-Mmarburgvirus Polymerase cofactor VP35 (a.a.31 to 329) | Q1PD52 | 2 µg | 1490 | |
RPN1141 | cDNA-Mmarburgvirus Matrix protein VP40 (a.a.31 to 303) | Q1PD51 | 2 µg | 1360 |
Mmarburgvirus cDNA and recombinant antigen
Mmarburgvirus is a highly virulent and pathogenic virus that belongs to the Filoviridae family. The virus encodes several important proteins that play crucial roles in the virus lifecycle and pathogenesis. These proteins include the membrane-associated protein VP24, the transcriptional activator VP30, the polymerase cofactor VP35, and the matrix protein VP40.
VP24 is a membrane-associated protein that plays a critical role in the assembly and egress of the virus particles. VP30 is a transcriptional activator that promotes the transcription of viral genes. VP35 is a polymerase cofactor that is required for viral RNA synthesis, and it also plays a role in modulating the host immune response. VP40 is a matrix protein that is involved in viral assembly and release.
Understanding the functions of these proteins is important for the development of effective strategies to prevent and treat Marburg virus infections. Research is ongoing to identify potential targets for antiviral drug development and vaccine design.
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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