Cet anticorps Souris Monoclonal détecte spécifiquement dans ELISA et WB. Il présente une réactivité envers Nipah Virus (NiV).
N° du produit ABIN7824739
Aperçu rapide pour Recombinant Nipah Virus Post-Fusion Glycoprotein (NIV pF) anticorps (ABIN7824739)
Antigène
Nipah Virus Post-Fusion Glycoprotein (NIV pF)
Type d'anticorp
Recombinant Antibody
Reactivité
Nipah Virus (NiV)
Hôte
Souris
Clonalité
Monoclonal
Conjugué
Inconjugué
Application
ELISA, Western Blotting (WB)
Clone
3C3
Expression System
HEK293
Fonction
Monoclonal Anti-Nipah Post Fusion glycoprotein Antibody, Human IgG1 (3C3) (MALS verified)
Attributs du produit
Monoclonal Anti-Nipah Post Fusion glycoprotein Antibody, Human IgG1 (3C3) is a chimeric monoclonal antibody recombinantly expressed from HEK293, which combines the variable region of a mouse monoclonal antibody with Human constant domain.
Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 with trehalose as protectant.
Conseil sur la manipulation
Please avoid repeated freeze-thaw cycles.
Stock
-20 °C,-80 °C
Stockage commentaire
For long term storage, the product should be stored at lyophilized state at -20°C or lower. This product is stable after storage at:
-20°C to -70°C for 12 months in lyophilized state;
-70°C for 3 months under sterile conditions after reconstitution.
Antigène
Nipah Virus Post-Fusion Glycoprotein (NIV pF)
Autre désignation
Nipah Virus Post-Fusion Glycoprotein
Sujet
Hendra virus (HeV) and Nipah virus (NiV) are henipaviruses discovered in the mid-to late 1990s that possess a broad host tropism and are known to cause severe and often fatal disease in both humans and animals. HeV and NiV infect host cells through the coordinated efforts of two envelope glycoproteins. The G glycoprotein attaches to cell receptors, triggering the fusion (F) glycoprotein to execute membrane fusion. G is a type II homotetrameric transmembrane protein responsible for binding to ephrinB2 or ephrinB3 (ephrinB2/B3) receptors. F is a homotrimeric type I transmembrane protein that is synthesized as a premature F0 precursor and cleaved by cathepsin L during endocytic recycling to yield the mature, disulfide-linked, F1 and F2 subunits. Upon binding to ephrinB2/B3, NiV G undergoes conformational changes leading to F triggering and insertion of the F hydrophobic fusion peptide into the target membrane. Subsequent refolding into the more stable post-fusion F conformation drives merger of the viral and host membranes to form a pore for genome delivery to the cell cytoplasm.