Recombinant Nipah Virus Post-Fusion Glycoprotein (NIV pF) antibody
Quick Overview for Recombinant Nipah Virus Post-Fusion Glycoprotein (NIV pF) antibody (ABIN7824739)
Target
Antibody Type
Reactivity
Host
Clonality
Conjugate
Application
Clone
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Expression System
- HEK293
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Purpose
- Monoclonal Anti-Nipah Post Fusion glycoprotein Antibody, Human IgG1 (3C3) (MALS verified)
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Characteristics
- 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.
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Purification
- Protein A purified / Protein G purified
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Purity
- 95% as determined by SDS-PAGE.
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Sterility
- 0.22 μm filtered
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Isotype
- IgG1, kappa
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Application Notes
- ELISA: 0.03-16 ng/ml; Western Blot: 0.05-10 µg/ml
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Restrictions
- For Research Use only
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Format
- Lyophilized
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Buffer
- Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 with trehalose as protectant.
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Handling Advice
- Please avoid repeated freeze-thaw cycles.
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Storage
- -20 °C,-80 °C
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Storage Comment
- 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.
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- Nipah Virus Post-Fusion Glycoprotein (NIV pF)
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Alternative Name
- Nipah Virus Post-Fusion Glycoprotein
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Background
- 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.
Target
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