Monoclonal Anti-Nipah virus (NiV) Glycoprotein G Antibody, Human IgG1 (5G9)

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Cat. No. / Size
Price
Availability
Qty
GLN-MY2257-100ug
$350.00
In Stock - Delivery in 2-3 business days
GLN-MY2257-1mg (500ug X 2)
$2310.00
In Stock - Delivery in 2-3 business days

Product Details

  • Source

    Chimeric Monoclonal Anti-Nipah virus (NiV) Glycoprotein G Antibody, Human IgG1 (5G9) is recombinantly expressed in HEK293. It consists of mouse variable regions genetically fused to human IgG1 constant domains.

  • Antibody Type

    Recombinant Monoclonal

  • Clone

    5G9

  • Isotype

    Human IgG1, Kappa

  • Host Species

    Mouse

  • Reactivity

    Virus

  • Immunogen

    Recombinant Nipah virus Glycoprotein G is expressed from human 293 cells

  • Specificity

    Specifically recognizes Nipah virus Glycoprotein G.

  • Application

    Application
    Recommended Usage
    Western Blot
    10-2 μg/mL
    ELISA
    0.2-2 μg/mL
  • Purification

    Protein A 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

     Glycoprotein G (NiV) ELISA

    Immobilized Nipah virus Glycoprotein G, His Tag (Cat. No. GLN-N52H3) at 1 μg/mL (100 μL/well) can bind Monoclonal Anti-Nipah virus (NiV) Glycoprotein G Antibody, Human IgG1 (5G9) (Cat. No. GLN-MY2257) with a linear range of 0.06-1 ng/mL (QC tested).

    Protocol
  • Western Blot

     Glycoprotein G (NiV) WESTERN BLOT
  • Western blot analysis of Nipah virus Glycoprotein G, His Tag (Cat. No. GLN-N52H3). The protein was loaded at 400 ng per lane and detected using Monoclonal Anti-Nipah virus (NiV) Glycoprotein G Antibody, Human IgG1 (5G9) at 2 μg/mL, followed by HRP-conjugated Goat Anti-Human IgG, Fcγ fragment specific secondary antibody at a 1:2000 dilution. A specific band was detected at approximately 80-100 kDa.

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FAQ

  • product

    Can lyophilized proteins remain stable during room-temperature shipping or temporary room-temperature exposure?

    In general, lyophilized proteins remain stable during room-temperature shipping or temporary exposure to room-temperature conditions.


    Many ACROBiosystems recombinant proteins are supplied in lyophilized (freeze-dried) form. The lyophilization process effectively removes moisture from the product, helping reduce degradation-related reactions and improve protein stability during transportation and storage.


    To evaluate the stability of lyophilized proteins under normal temperature conditions, ACROBiosystems conducted a stability study on 11 representative lyophilized protein products at 37°C. The study demonstrated that these proteins maintained good quality stability after storage at 37°C for approximately 20 days. Based on these validation results, temporary room-temperature exposure during shipping or handling is generally not expected to have a significant impact on product quality or downstream application performance.


    To ensure optimal long-term stability, products should be stored according to the storage conditions specified in the product Certificate of Analysis (COA) upon receipt.


    Supporting Document


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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