The F Antibody (PACO34134) is a highly specific and sensitive monoclonal antibody designed for research involving the F protein, a critical component of certain viruses. This antibody, produced using advanced technology, is ideal for detecting and studying the F protein in various samples, making it invaluable for research in virology and infectious diseases.The F protein is essential for the entry of viruses into host cells and plays a crucial role in virus replication and infectivity. Understanding the function and structure of the F protein is essential for developing antiviral therapies and vaccines. The F Antibody (PACO34134) provides researchers with a powerful tool for investigating the mechanisms of viral infection and developing strategies to combat viral diseases.
This monoclonal antibody is highly specific to the F protein and has been rigorously validated for use in immunofluorescence, immunohistochemistry, and other immunological techniques. Its exceptional sensitivity and specificity make it a valuable asset for researchers studying viral pathogenesis, vaccine development, and antiviral drug discovery. Don't miss out on the opportunity to enhance your research with the F Antibody (PACO34134) from AssayGenie.
Antibody Name:
F Antibody (PACO34134)
Antibody SKU:
PACO34134
Size:
50ug
Host Species:
Rabbit
Tested Applications:
ELISA
Recommended Dilutions:
Species Reactivity:
Canine distemper virus
Immunogen:
Recombinant Canine distemper virus Fusion glycoprotein F0 protein (136-608AA)
Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) probably interacts with H at the virion surface. Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis.
Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) probably interacts with H at the virion surface. Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis ().
