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Cat# | Product Name | Swiss Prot# | Size | Price (US$) | Order |
PN0233 | Recombinant Protein-Cercopithecine herpesvirus 1 Envelope glycoprotein D (a.a.18 to 342) | P36342 | 100 µg | 1195 | |
PN0234 | Recombinant Protein-Cercopithecine herpesvirus 1 Envelope glycoprotein I (a.a.23 to 109) | P36343 | 100 µg | 1195 | |
PN0235 | Recombinant Protein-Cercopithecine herpesvirus 1 Capsid protein VP23 (a.a.33 to 318) | Q7T5E5 | 100 µg | 1195 | |
PN0236 | Recombinant Protein-Cercopithecine herpesvirus 1 Immediate early protein ICP27 (a.a.31 to 490) | Q805X4 | 100 µg | 1195 | |
PN0237 | Recombinant Protein-Cercopithecine herpesvirus 2 Scaffolding protein (a.a.21 to 292) | Q5Y0S6 | 100 µg | 1195 | |
PN0238 | Recombinant Protein-Cercopithecine herpesvirus 2 Minor capsid protein (a.a.21 to 577) | Q5Y0S8 | 100 µg | 1195 | |
PN0239 | Recombinant Protein-Cercopithecine herpesvirus 2 Capsid protein (a.a.100 to 500) | Q5Y0U7 | 100 µg | 1195 | |
PN0240 | Recombinant Protein-Cercopithecine herpesvirus 9 Simian varicella virus Envelope glycoprotein E (a.a.25 to 526) | Q04548 | 100 µg | 1195 | |
PN0241 | Recombinant Protein-Cercopithecine herpesvirus 9 Simian varicella virus Envelope glycoprotein I (a.a.21 to 274) | Q04547 | 100 µg | 1195 | |
RPN0233 | cDNA-Cercopithecine herpesvirus 1 Envelope glycoprotein D (a.a.18 to 342) | P36342 | 2 µg | 1620 | |
RPN0234 | cDNA-Cercopithecine herpesvirus 1 Envelope glycoprotein I (a.a.23 to 109) | P36343 | 2 µg | 800 | |
RPN0235 | cDNA-Cercopithecine herpesvirus 1 Capsid protein VP23 (a.a.33 to 318) | Q7T5E5 | 2 µg | 1425 | |
RPN0236 | cDNA-Cercopithecine herpesvirus 1 Immediate early protein ICP27 (a.a.31 to 490) | Q805X4 | 2 µg | 2295 | |
RPN0237 | cDNA-Cercopithecine herpesvirus 2 Scaffolding protein (a.a.21 to 292) | Q5Y0S6 | 2 µg | 1355 | |
RPN0238 | cDNA-Cercopithecine herpesvirus 2 Minor capsid protein (a.a.21 to 577) | Q5Y0S8 | 2 µg | 2780 | |
RPN0239 | cDNA-Cercopithecine herpesvirus 2 Capsid protein (a.a.100 to 500) | Q5Y0U7 | 2 µg | 2000 | |
RPN0240 | cDNA-Cercopithecine herpesvirus 9 Simian varicella virus Envelope glycoprotein E (a.a.25 to 526) | Q04548 | 2 µg | 2505 | |
RPN0241 | cDNA-Cercopithecine herpesvirus 9 Simian varicella virus Envelope glycoprotein I (a.a.21 to 274) | Q04547 | 2 µg | 1265 |
Cercopithecine herpesvirus cDNA and recombinant antigen
CHV also known as Herpes B virus, is a type of herpesvirus that infects non-human primates, such as macaques, guenons, and mangabeys. This virus is transmitted through contact with contaminated bodily fluids, such as saliva or nasal secretions, or through bites from infected primates. Cercopithecine herpesvirus causes a potentially fatal disease in non-human primates and can also be transmitted to humans, causing severe encephalitis (brain inflammation). The genome of Cercopithecine herpesvirus is a double-stranded DNA molecule that is approximately 150 kilobases in length. The genome encodes several proteins that are involved in various functions, such as replication, evasion of host immunity, and pathogenesis. There is currently no specific cure for Cercopithecine herpesvirus infections, and management is primarily supportive. However, it is important for people who work with non-human primates to take precautions to prevent transmission of this virus.
The genome of CHV is a double-stranded DNA molecule that is approximately 150 kilobases in length. The genome encodes several proteins that are involved in various functions, such as replication, evasion of host immunity, and pathogenesis. The virus replicates in the nucleus of infected cells and is transmitted from host to host through contact with contaminated bodily fluids, such as saliva or nasal secretions, or through bites from infected primates. Cercopithecine herpesvirus causes a potentially fatal disease in non-human primates and can also be transmitted to humans, causing severe encephalitis (brain inflammation). There is currently no specific cure for Cercopithecine herpesvirus infections, and management is primarily supportive. However, it is important for people who work with non-human primates to take precautions to prevent transmission of this virus.
The antigens of CHV are recognized by the host’s immune system and can elicit the production of antibodies that neutralize the virus. Antigens play an important role in the development of diagnostic tests for CHV, as they are used to detect the presence of antibodies against the virus in the blood of infected animals or humans. The antigenic properties of Cercopithecine herpesvirus are also important in the design of vaccines, as they are used to stimulate the immune system and protect against future infections with this virus.
Envelope glycoprotein D (gD) is a viral protein that plays a key role in the entry of the virus into host cells by binding to specific host cell receptors.
Envelope glycoprotein I (gI) is another viral protein that is involved in the entry of the virus into host cells, and it interacts with gD to enhance the efficiency of viral entry.
VP23 is a capsid protein that is involved in the formation of the capsid, which encloses the viral genome and protects it from host defenses.
ICP27 is an immediate-early viral protein that is involved in the regulation of viral gene expression, and it plays a critical role in the replication of the virus.
The scaffolding protein is a viral protein that is involved in the assembly of the capsid, and it is responsible for maintaining the structural integrity of the capsid during the assembly process.
Minor capsid protein is a viral protein that is also involved in the formation of the capsid and plays a role in the maturation of the virus.
Capsid protein is another viral protein that is the major structural protein of the virus and forms the outer shell of the viral particle.
Envelope glycoprotein E is a viral protein that is involved in the release of newly formed viral particles from infected cells and is also involved in viral entry into host cells.
It is important to note that Cercopithecine herpesvirus has a complex genome that encodes numerous other viral proteins, including enzymes, regulatory proteins, and accessory proteins, all of which play critical roles in viral replication, pathogenesis, and immune evasion.
Understanding the structure and function of these viral proteins is important for understanding the pathogenesis of herpesvirus infections and developing effective treatments and prevention strategies. Research into these proteins may lead to the development of new diagnostic tests, vaccines, and antiviral therapies for these 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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