Protein is >95% pure as determined by SDS-PAGE
The E.Coli derived recombinant protein contains the HSV-2 gD (525-578) immunodominant region.
HSV2 gD is fused to a six histidine his tag at c-terminus and purified by proprietary chromatographic techniques.
Herpes simplex virus (HSV) enters host cells through a multi-step process that involves interactions between viral glycoproteins and cell surface receptors. These interactions facilitate the fusion of the viral envelope with the host cell membrane, creating pores through which viral particles gain entry. This mechanism is similar to the entry pathways employed by other viruses.
This recombinant protein consists of the immunodominant region (amino acids 525-578) of HSV-2 glycoprotein D (gD). It is produced in E. coli and purified using proprietary chromatographic methods. A six-histidine tag is fused to the C-terminus to facilitate purification.
SDS-PAGE analysis indicates that the protein purity exceeds 95%.
The protein is supplied at a concentration of 1 mg/ml in 1x phosphate-buffered saline (PBS).
For short-term storage (up to one week), HSV-2 gD can be kept at 4°C. For long-term storage, it is recommended to store the protein below -18°C. Avoid repeated freeze-thaw cycles to maintain protein stability.
This product is suitable for use in enzyme-linked immunosorbent assays (ELISA) and Western blotting (WB).
Herpes Simplex Virus-2 (HSV-2) is a significant human pathogen responsible for genital herpes, a common sexually transmitted infection. The virus contains several glycoproteins on its surface, which play crucial roles in its ability to infect host cells and evade the immune system. One of these glycoproteins is glycoprotein D (gD), which is essential for the virus’s entry into host cells and cell-to-cell spread.
Glycoprotein D (gD) is a surface protein found on HSV-2 that interacts with host cell receptors to facilitate viral entry. The specific region of gD spanning amino acids 525-578 is of particular interest due to its role in the virus’s infectivity and immune evasion mechanisms. This region is often targeted in vaccine development and therapeutic research.
Recombinant gD (525-578 a.a.) refers to a laboratory-produced version of this specific segment of the glycoprotein. Recombinant proteins are created by inserting the gene encoding the protein of interest into an expression system, such as bacteria or yeast, which then produces the protein. This method allows for the production of large quantities of the protein for research and therapeutic purposes.
The development of vaccines against HSV-2 has been a significant focus of research due to the virus’s prevalence and the lack of a cure. Recombinant gD has been a key component in several vaccine candidates. Studies have shown that vaccines containing recombinant gD can elicit strong immune responses, including the production of neutralizing antibodies and cell-mediated immunity .
In addition to vaccine development, recombinant gD (525-578 a.a.) has potential therapeutic applications. It can be used to study the immune response to HSV-2 and to develop therapies that target the virus’s ability to infect host cells. For example, recombinant gD can be used to screen for antibodies that block the interaction between the virus and host cell receptors, potentially leading to new antiviral treatments .