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Andes Virus Glycoprotein Gn Head (C-His)

Cat # Size Price Quantity
60680125 μg$300
606802100 μg$785

  Bulk/Custom

Product Details

ApplicationELISA, BLI
FormatLiquid, Purified
Expression HostCHO
Target NameAndes virus glycoprotein Gn Head, Andes virus Gn protein, ANDV Gn glycoprotein, Andes orthohantavirus glycoprotein Gn, Hantavirus envelope glycoprotein Gn, G1 glycoprotein
SpeciesAndes Virus
accession numberAF291703.2
SourcesRecombinant Andes Virus Glycoprotein Gn Head (Met19–Glu374) with a C-terminal histidine tag is expressed in CHO cells. The protein is derived from the Andes virus strain Chile-9717869.
Molecular WeightThis protein has a predicted molecular weight of 39–41 kDa (without glycosylation).
Affinity TagC-His
Purity>95% based on SDS-PAGE under reducing condition
Regulatory StatusRUO
Formulation1xPBS buffer, pH7.4, 0.22 µm filtered
Endotoxin levelNot tested
Protein Concentration25µg size is bottled at 0.2mg/mL concentration. 100 µg size is supplied at a lot-specific concentration.
Storage and HandlingBriefly centrifuge the vial upon receipt. An unopened vial can be stored at 4°C for up to 2 weeks, or at -20°C or below for up to six months. The protein may be further diluted to 0.1 mg/mL using 0.22 µm-filtered PBS buffer (pH 7.4). For long-term storage, the diluted stock solution should be aliquoted and stored at ≤ –70°C to minimize freeze-thaw cycles. If additional dilution is required, carrier proteins such as FBS or BSA should be added to maintain protein stability.
Research AreasHantavirus, Infectious Diseases

Background Information

Andes virus (ANDV) is an enveloped negative-sense RNA virus belonging to the genus Orthohantavirus within the family Hantaviridae. Andes virus is one of the major causative agents of hantavirus cardiopulmonary syndrome (HCPS) in South America and is notable for its documented human-to-human transmission capability.
The viral surface glycoprotein precursor (GPC) is proteolytically processed into the Gn and Gc envelope glycoproteins, which mediate viral attachment, host-cell entry, membrane fusion, and immune recognition. The Gn head domain is highly exposed on the virion surface and serves as a major target for neutralizing antibodies. Recombinant Andes Virus Gn Head Protein is widely used in antiviral antibody discovery, vaccine research, serological assay development, epitope mapping, and structural biology studies.

Learn more about Andes Virus in our detailed Infographic.

Data Sheets

Andes Virus Glycoprotein Gn Head (C-His) TDS

Related Protocols

Direct ELISA Protocol

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Frequently Asked Questions

Why are Recombinant Proteins expressed with epitope tags?
The majority of InnoCyto's recombinantly expressed proteins are engineered with a short, well-characterized peptide sequence (e.g., His-tag, Fc-tag, Flag-tag, or similar) fused to the protein of interest. The tag enables reliable detection, purification, or immobilization of the protein using commercially available anti-tag antibodies or affinity resins, without needing a custom antibody against the native protein.
What types of tagged proteins are best for my application?
Common tag options include His-tag (for affinity purification via Ni-NTA/IMAC and detection via anti-His antibodies), Fc-tag (for use in binding assays, ELISA capture, and dimerization studies), and Flag-tag (for high-specificity detection and immunoprecipitation). Tag choice should be based on your intended workflow — purification-focused work often favors His-tag, while functional binding or capture-based assays often benefit from Fc-tag.
Does the tag affect the protein's biological activity or binding function?
Tag placement (N-terminal vs. C-terminal) and type are selected during design to minimize interference with the protein's native folding and functional binding site, and each tagged protein is validated for activity in relevant binding or functional assays. Product pages indicate the tag location and confirm the functional validation performed for that specific protein.

Have a product or application question? Consult our FAQs or contact us.