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Recombinant Hendra Virus Glycoprotein G (G), N-Strep

Cat. No.VG9C355

Product TypeVeterinary Antigens

Size

Product Overview

BioVenic's Recombinant Hendra Virus Glycoprotein G (G), N-Strep is a recombinant protein expressed from E.coli. Its predicted molecular weight is 63.2 kDa. The purity is>90% (SDS-PAGE).

Specifications

Type Recombinant Protein
Species Virus
Expression System E.coli
Purity >90% (SDS-PAGE)
Predicted Molecular Weight 63.2 kDa
Physical State Lyophilized
Formulation The buffer before lyophilization is a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.

Target Information

In veterinary medicine, the function of Hendra virus glycoprotein G (G) is to act as the virus's attachment protein, responsible for binding the virus to host cell surface receptors, initiating the infection process. The G protein engages with host cell membrane protein receptors such as ephrin-B2 and -B3, and this initial interaction is believed to be sufficient to trigger the F-mediated fusion event between the viral envelope and the host cell membrane leading to virus entry. Furthermore, the G protein is a primary target for neutralizing antibodies and is crucial for vaccine development and antiviral treatment strategies.

Protein Hendra Virus Glycoprotein G (G)
Protein Synonym Glycoprotein G; G
UniProt ID O89343

Shipping and Storage

This product is shipped with dry ice. Avoid repeated freezing and thawing. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use.

Documents

COA

To request a Certificate of Analysis, please enter the Lot No. in the search box. Note: Certificate of Analysis not available for kits.

The product is for research use only.
Not for commercial, prophylactic, diagnostic, or therapeutic applications.

User Note

  1. Always centrifuge tubes before opening. Avoid mixing by vortexing or pipetting. Reconstitute to a concentration more than 100 μg/ml is recommended. Dissolve the lyophilized protein in distilled water.Aliquote the reconstituted solution to minimise freeze-thaw cycles.
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