Biotinylated Nipah virus Fusion glycoprotein, His Tag, ultra sensitivity (primary amine labeling)

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FUN-N82H3-25ug
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FUN-N82H3
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Synonyms

Fusion glycoprotein, F protein, F, Nipah virus, Hendra virus

Source

Biotinylated Nipah virus Fusion glycoprotein, His Tag, primary amine labeling (FUN-N82H3) is expressed from human 293 cells (HEK293). It contains AA Ile 27 - Ser 487 (Accession # Q9IH63-1). It is the biotinylated form of Nipah virus Pre-Fusion glycoprotein, His Tag (Cat. No. FUN-N52H3).

Predicted N-terminus: Ile 27

Molecular Characterization

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

The protein has a calculated MW of 55.9 kDa. The protein migrates as 55-65 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE) due to glycosylation.

Labeling

The primary amines in the side chains of lysine residues and the N-terminus of the protein are conjugated with biotins using standard chemical labeling method. A standard biotin reagent (13.5 angstroms) is used in this product.

Protein Ratio

Passed as determined by the HABA assay / binding ELISA.

Purity

>90% as determined by SDS-PAGE.

Formulation

Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 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.

Shipping and Storage

This product is shipped at ambient temperature.

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:
  • -20°C to -70°C for 12 months in lyophilized state;
  • -70°C for 3 months under sterile conditions after reconstitution.

Background Introduction

Hendra virus (HeV) and Nipah virus (NiV) are henipaviruses discovered in the mid-to late 1990s that possess a broad host tropism and are known to cause severe and often fatal disease in both humans and animals. HeV and NiV infect host cells through the coordinated efforts of two envelope glycoproteins. The G glycoprotein attaches to cell receptors, triggering the fusion (F) glycoprotein to execute membrane fusion. G is a type II homotetrameric transmembrane protein responsible for binding to ephrinB2 or ephrinB3 (ephrinB2/B3) receptors. F is a homotrimeric type I transmembrane protein that is synthesized as a premature F0 precursor and cleaved by cathepsin L during endocytic recycling to yield the mature, disulfide-linked, F1 and F2 subunits. Upon binding to ephrinB2/B3, NiV G undergoes conformational changes leading to F triggering and insertion of the F hydrophobic fusion peptide into the target membrane. Subsequent refolding into the more stable post-fusion F conformation drives merger of the viral and host membranes to form a pore for genome delivery to the cell cytoplasm.