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Hendra virus Glycoprotein, His Tag (MALS verified)

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Cat. No. / Size
Price
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GLN-H52H3-50ug
$465.00
GLN-H52H3-500ug
$3170.00
ETA of in-stock products:2 business days
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Product Details

  • Synonyms

    Glycoprotein G (HeV)

  • Source

    Hendra virus Glycoprotein, His Tag (GLN-H52H3) is expressed from human 293 cells (HEK293). It contains AA Gln 71 - Ser 604 (Accession # O89343-1).

    Predicted N-terminus: His

    Request for sequence
  • Molecular Characterization

    Glycoprotein G (HeV) Structure

    Other Tags and Version Biotin & Other Labeled Version

    This protein carries a polyhistidine tag at the N-terminus.

    The protein has a calculated MW of 61.5 kDa. The protein migrates as 80-100 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE) due to glycosylation.

  • Endotoxin

    Less than 1.0 EU per μg by the LAL method / rFC method.

  • Purity

    >95% as determined by SDS-PAGE.

  • Formulation

    Lyophilized from 0.22 μm filtered solution in PBS, 0.3 M Arginine, pH7.4 with trehalose as protectant.

    Contact us for customized product form or formulation.

  • Reconstitution

    Please see Certificate of Analysis for specific instructions.

    For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

  • Storage

    For long term storage, the product should be stored at 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.
  • ACRO Quality Management System

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

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Performance Data

  • SDS-PAGE

    Glycoprotein G (HeV) SDS-PAGE

    Hendra virus Glycoprotein, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 95% (With Star Ribbon Pre-stained Protein Marker).

  • SEC-MALS

    Glycoprotein G (HeV) SEC-MALS

    The purity of Hendra virus Glycoprotein, His Tag (Cat. No. GLN-H52H3) is more than 85% and the molecular weight of this protein is around 70-100 kDa verified by SEC-MALS.

    Report
  • Bioactivity-ELISA

     Glycoprotein G (HeV) ELISA

    Immobilized Hendra virus Glycoprotein, His Tag (Cat. No. GLN-H52H3) at 5 μg/mL (100 μL/well) can bind Human Ephrin-B2 Protein, Fc tag (Cat. No. EPN-H5259) with a linear range of 0.1-2 ng/mL (QC tested).

    Protocol
  •  Glycoprotein G (HeV) ELISA

    Immobilized Hendra virus Glycoprotein, His Tag (Cat. No. GLN-H52H3) at 1 μg/mL (100 μL/well) can bind Anti-Nipah/Hendra Glycoprotein G Antibody, Human IgG1 with a linear range of 0.03-1 ng/mL (Routinely tested).

    Protocol
  • Bioactivity-SPR

     Glycoprotein G (HeV) SPR

    Anti-Nipah/Hendra Glycoprotein G Antibody, Human IgG1 captured on Protein A Chip can bind Hendra virus Glycoprotein, His Tag (Cat. No. GLN-H52H3) with an affinity constant of 12.3 nM as determined in a SPR assay (Biacore 8K) (Routinely tested).

    Protocol

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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.

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