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Nipah virus Glycoprotein G, His Tag (MALS verified)

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.

Product Specifications

Background

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.

Specifications

This protein carries a polyhistidine tag at the N-terminus. The protein has a calculated MW of 61.2 kDa. The protein migrates as 70-100 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE) due to glycosylation.

Accession Number

Q9IH62-1

Expression Region

Gln 71 - Thr 602

Host

HEK293

Target

Glycoprotein G (NiV)

Conjugation

Unconjugated

Tag

N-10xHis

Source

Nipah virus

Stability

-20°C to -70°C for 12 months in lyophilized state; -70°C for 3 months under sterile conditions after reconstitution. For long term storage, the product should be stored at lyophilized state at -20°C or lower.

Endotoxin

1.0 EU per μg

Purity

95%

Bioactivity

Immobilized Nipah virus Glycoprotein G, His Tag (Cat. No. GLN-N52H3) at 5 μg/mL (100 μL/well) can bind Human Ephrin-B2 Protein, Fc tag (Cat. No. EPN-H5259) with a linear range of 0.1-2 ng/mL (QC tested).

Format

Powder

Buffer

PBS, pH7.4

Additives

Trehalose

Molecular Weight

61.2 kDa

Additionnal Information

Please see 'Shipping-and-Payments' sheet. Website: https://www.acrobiosystems.com/support/shipping-and-payments

Shipping Conditions

RT

Storage Conditions

-20°C

Package Size

50ug*1

Host or Source

HEK293

Species

Nipah virus

Protein ID

Q9IH62-1

Preservative

Trehalose

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