Monoclonal Anti-Nipah Post Fusion glycoprotein Antibody, Human IgG1 (3C3) (MALS verified)

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Cat. No. / Size
Price
Qty
NIN-M760-100ug
$415.00
NIN-M760-1mg
$2735.00
ETA of in-stock products:2 business days

Product Details

  • Source

    Monoclonal Anti-Nipah Post Fusion glycoprotein Antibody, Human IgG1 (3C3) is a chimeric monoclonal antibody recombinantly expressed in HEK293, which combines the variable region of a mouse monoclonal antibody with human constant domain.

  • Antibody Type

    Recombinant Monoclonal

  • Clone

    3C3

  • Isotype

    Human IgG1, Kappa

  • Host Species

    Mouse

  • Specificity

    This product is a specific antibody specifically reacts with Nipah Post Fusion glycoprotein.

  • Application

    Application
    Recommended Usage
    Western Blot
    0.05-10 ug/mL
  • Purification

    Protein A purified / Protein G purified.

  • Aggregation

    Less than 10%, as determined by SEC-MALS.

  • Concentration

    Please refer to the Certificate of Analysis (CoA).

  • Form

    Lyophilized

  • Formulation

    Lyophilized from a 0.22 μm-filtered solution in PBS (pH 7.4), with trehalose as protectant.

    Please contact us for customized product forms or formulations.

  • Reconstitution

    Please refer to the Certificate of Analysis (CoA) for specific instructions.

  • Shipping

    Lyophilized product is shipped at ambient temperature.

  • Storage

    For long term storage, the product should be stored in a lyophilized state at -20°C or lower.

    Please avoid repeated freeze-thaw cycles.

    This product is stable after storage at:

    1. -20°C to -70°C for 12 months in lyophilized state;
    2. -70°C for 3 months under sterile conditions after reconstitution.
  • Notices

    Product Specific Notices: For research use only.

  • ACRO Quality Management System

    1. QMS(ISO, GMP)
    2. Quality Advantages
    3. Quality Control Process

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Performance Data

  • Bioactivity-ELISA

     Postfusion glycoprotein F0/post-F protein (NiV) ELISA

    Immobilized Nipah virus Post-Fusion glycoprotein, His Tag (Cat. No. PON-V52H3) at 1 μg/mL (100 μL/well) can bind Monoclonal Anti-Nipah Post Fusion glycoprotein Antibody, Human IgG1 (3C3) (Cat. No. NIN-M760) with a linear range of 0.03-1 ng/mL (QC tested).

    Protocol
  • Bioactivity-SPR

     Postfusion glycoprotein F0/post-F protein (NiV) SPR

    Monoclonal Anti-Nipah Post Fusion glycoprotein Antibody, Human IgG1 (3C3) (Cat. No. NIN-M760) captured on Protein A Chip can bind Nipah virus Post-Fusion glycoprotein, His Tag (Cat. No. PON-V52H3) with an affinity constant of 0.937 nM as determined in a SPR assay (Biacore 8K) (Routinely tested).

    Protocol

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FAQ

  • Product

    What do “pre” and “post” refer to in the names of viral proteins?

    In virology, “pre” refers to the conformation of a viral surface glycoprotein before fusion with the host cell membrane, while “post” refers to the conformation after membrane fusion and entry into the host cell. Both are naturally occurring states in the viral life cycle. Because the “pre” conformation represents a critical stage before viral entry, antibodies designed against this state often exhibit stronger neutralizing activity and are therefore more effective in preventing infection.

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.

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