The Outer Capsid Glycoprotein VP7 Antibody (PACO34126) is a valuable tool for researchers studying viral pathogens, specifically those with outer capsid glycoproteins like VP7. This antibody, produced in rabbits, is highly specific and reactive with samples from a variety of species, making it ideal for use in immunofluorescence and immunohistochemistry applications.VP7 is a key component of the outer capsid of certain viruses, playing a critical role in viral attachment and entry into host cells. By targeting VP7 with this antibody, researchers can investigate viral infection mechanisms, pathogenesis, and potential therapeutic interventions.
The high specificity and sensitivity of this antibody make it a reliable tool for studying viral biology and developing antiviral strategies.Furthermore, understanding the structure and function of VP7 can provide valuable insights into viral evolution, transmission, and host immunity. By utilizing the Outer Capsid Glycoprotein VP7 Antibody (PACO34126) in their research, scientists can unlock new knowledge about viral pathogens and explore novel approaches for preventing or treating viral infections.
Calcium-binding protein that interacts with rotavirus cell receptors once the initial attachment by VP4 has been achieved. Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. Following entry into the host cell, low intracellular or intravesicular Ca2+ concentration probably causes the calcium-stabilized VP7 trimers to dissociate from the virion. This step is probably necessary for the membrane-disrupting entry step and the release of VP4, which is locked onto the virion by VP7.
Synonyms:
Outer capsid glycoprotein VP7
UniProt Protein Function:
Outer capsid protein involved in attachment and possibly entry into the host epithelial cell. It is subsequently lost, together with VP4, following virus entry into the host cell. The outer layer contains 780 copies of VP7, grouped as 260 trimers. Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. In integrin-dependent strains, VP7 seems to essentially target the integrin heterodimers ITGAX/ITGB2 and ITGA5/ITGB3 at a postbinding stage, once the initial attachment by VP4 has been achieved ().
