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Rabies virus (strain CVS-11) Glycoprotein G, His Tag (MALS verified)

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Cat. No. / Size
Price
Qty
RAG-V55H5-50ug
$465.00
RAG-V55H5-500ug (250ug X 2)
$2885.00
RAG-V55H5-1mg (250ug X 4)
$4820.00
ETA of in-stock products:2 business days
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Product Details

  • Synonym

    Glycoprotein/G Protein (RABV)

  • Source

    Rabies virus (strain CVS-11) Glycoprotein G, His Tag (RAG-V55H5) is expressed from Baculovirus-Insect cells. It contains AA Lys 20 - Lys 458 (Accession # ADJ29911.1).

    Predicted N-terminus: Lys 20

    Request for sequence
  • Molecular Characterization

    Glycoprotein/G Protein (RABV) Structure

    Other Tags and Version Biotin & Other Labeled Version

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

    The protein has a calculated MW of 53.6 kDa. The protein migrates as 60-65 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE) due to glycosylation.

    Within the expressed region, several mutations were introduced to optimize the protein expression and stability.

    The protein is designed as a trimer.

  • 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 0.1 M Sodium citrate, pH5.5 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 Protein (RABV) SDS-PAGE

    Rabies virus (strain CVS-11) Glycoprotein G, 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 Protein (RABV) SEC-MALS

    The purity of Rabies virus (strain CVS-11) Glycoprotein G, His Tag (Cat. No. RAG-V55H5) is more than 85% and the molecular weight of this protein is around 165-230 kDa verified by SEC-MALS.

    Report
  • Bioactivity-ELISA

     Glycoprotein/G Protein (RABV) ELISA

    Immobilized Rabies virus (strain CVS-11) Glycoprotein G, His Tag (Cat. No. RAG-V55H5) at 1 μg/mL (100 μL/well) can bind Mouse Glycoprotein G Antibody, Mouse IgG1 (523-11) (Cat. No. RAG-M305) with a linear range of 0.1-2 ng/mL (QC tested).

    Protocol
  • Bioactivity-SPR

     Glycoprotein/G Protein (RABV) SPR

    Monoclonal Anti-Glycoprotein G(Lyssavirus rabies) Antibody, Human IgG1 (4A7) (Cat. No. GLN-M645) captured on Protein A Chip can bind Rabies virus Glycoprotein G, His Tag (Cat. No. RAG-V55H5) with an affinity constant of 1.25 nM as determined in a SPR assay (Biacore 8K) (Routinely tested).

    Protocol

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Background

Rabies virus (RABV), scientific name Rabies lyssavirus, is a deadly neurotropic virus that causes rabies in humans and animals. Rabies virus has an extremely wide host range and its transmission most often occur through the saliva of animals. Without intervention prior to disease progression, rabies has the highest case fatality of any infectious disease. RABV contains a single-stranded negative-sense RNA genome that encodes five structural proteins: nucleoprotein (N), phosphoprotein (P), matrix protein (M), glycoprotein (G), and RNA-dependent RNA polymerase (L). Among these viral proteins, the RABV glycoprotein (RABV-G) is a pivotal player mediating virus entry and the major target of neutralizing antibodies, thus a key factor for vaccine and drug design.

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