HSV-1 gD (84-175)
Protein is >95% pure as determined by SDS-PAGE
Description
The E.Coli derived recombinant protein contains the HSV-1 gD (84-175) immunodominant region.
Product Specs
Product Science Overview
Herpes Simplex Virus-1 (HSV-1) is a prevalent human pathogen known for causing oral and genital herpes. The virus has a complex structure and lifecycle, which includes both lytic and latent phases. One of the critical components of HSV-1 is glycoprotein D (gD), which plays a pivotal role in the virus’s ability to enter host cells.
Glycoprotein D (gD) is an essential envelope protein of HSV-1. It is involved in the initial stages of viral infection by mediating the virus’s attachment and entry into host cells. The gD protein interacts with specific receptors on the surface of host cells, facilitating the fusion of the viral envelope with the host cell membrane.
The recombinant form of HSV-1 gD, specifically the amino acid region 84-175, is a truncated version of the full-length protein. This region is known to contain immunodominant epitopes, which are crucial for eliciting an immune response. The recombinant gD (84-175 a.a.) is often produced in E. coli and used in various research and diagnostic applications .
- Vaccine Development: The recombinant gD (84-175 a.a.) is a key component in the development of vaccines against HSV-1. Its immunodominant epitopes make it an ideal candidate for inducing protective immunity.
- Diagnostic Tools: This recombinant protein is used in serological assays to detect HSV-1 infections. It helps in identifying the presence of antibodies against HSV-1 in patient samples.
- Research: The recombinant gD (84-175 a.a.) is widely used in research to study the mechanisms of HSV-1 entry and immune evasion. It serves as a valuable tool for understanding the virus’s interaction with host cells and the host immune response.
The production of recombinant gD (84-175 a.a.) typically involves cloning the gene segment encoding this region into an expression vector, which is then introduced into E. coli cells. The bacteria are cultured, and the recombinant protein is expressed and purified using various chromatographic techniques. The purified protein is then used in downstream applications .
