Recombinant Nipah virus/NiV F/Fusion glycoprotein F0 Protein, N-His-SUMO & C-Strep

Recombinant Nipah virus/NiV F/Fusion glycoprotein F0 Protein, N-His-SUMO & C-Strep

Cat. No.: PEX10965
Size:50μg price2:$272
Size:500μg price3:$401
Category: Nipah virus Proteins Tags: , ,
Name

Recombinant Nipah virus/NiV F/Fusion glycoprotein F0 Protein, N-His-SUMO & C-Strep

Purity

>90% as determined by SDS-PAGE.

Endotoxin level

Please contact with the lab for this information.

Construction

Ile27-Gly112

Accession #

Q9IH63

Host

E. coli

Species

Nipah virus (NiV)

Predicted Molecular Mass

23.21 kDa

Buffer

0.01M PBS, pH 7.4.

Form

Lyophilized

Shipping

In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise.

Stability&Storage

Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt.

Reconstitution

Always centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.

 

 

 

Alternative Names

Nipah virus/NiV F/Fusion glycoprotein F0 Protein

 

Background

Nipah virus (NiV), a highly pathogenic zoonotic paramyxovirus, mediates host cell entry through the coordinated action of two envelope glycoproteins: the attachment glycoprotein (G), which engages the host cell receptors ephrin-B2 and ephrin-B11, and the fusion glycoprotein (F), which drives membrane fusion following receptor binding. These viral surface proteins, along with the viral RNA-dependent RNA polymerase (RdRp) complex comprising the nucleoprotein (N), phosphoprotein (P), and large polymerase protein (L), constitute the primary molecular targets for therapeutic intervention and vaccine development. The conserved receptor-binding interface of the G protein and the fusion machinery of the F protein represent particularly attractive targets for neutralizing antibodies and entry inhibitors, while the viral replication machinery offers potential targets for broad-spectrum antiviral compounds targeting paramyxovirus transcription and replication.

 

Note

For Research Use Only , Not for Diagnostic Use.

 

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