Andes Virus Glycoprotein Gc (H953F) (C-His)

Cat # Size Price Quantity
60700125 μg$300
607002100 μg$798

Product Details


ApplicationELISA, BLI
FormatLiquid, Purified
Expression HostCHO
Target NameAndes virus glycoprotein Gc, Andes virus Gc protein, ANDV Gc glycoprotein, Andes orthohantavirus glycoprotein Gc, Hantavirus envelope glycoprotein Gc, G2 glycoprotein
SpeciesAndes Virus
accession numberAF291703.2
SourcesRecombinant Andes Virus Glycoprotein Gc (Glu652-Asn1107) (H953F) 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 50–52 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.

Background Information


Andes virus (ANDV) is a member of the genus Orthohantavirus in the family Hantaviridae and is a major etiological agent of hantavirus cardiopulmonary syndrome (HCPS) in South America. Unlike most hantaviruses, Andes virus has demonstrated the ability for person-to-person transmission, making it a significant emerging infectious disease threat.
The Andes virus glycoprotein precursor (GPC) is proteolytically cleaved into the envelope glycoproteins Gn and Gc. The Gc glycoprotein is a class II viral fusion protein responsible for mediating fusion between the viral envelope and host-cell membrane during viral entry. Gc also serves as an important target for neutralizing antibodies and antiviral therapeutics. Recombinant Andes Virus Glycoprotein Gc is widely used in studies of viral entry, membrane fusion, structural biology, epitope mapping, serological assay development, and antibody discovery.

Learn more about Andes Virus in our detailed Infographic.

Data Sheets


Andes Virus Glycoprotein Gc (H953F) (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.