Glycoprotein/G Protein, HRSV (232a.a, HEK293, His)

Glycoprotein/G Protein, HRSV (232a.a, HEK293, His) is the recombinant virus-derived Glycoprotein/G protein, expressed by HEK293, with N-His tag.

The G protein backbone contains 289 to 299 amino acids (32-33 kDa), depending on the strain, and is palmitoylated. It has no sequence homology with other paramyxovirus attachment proteins, and no hemagglutinating or neuraminidase functions. The G protein has 30-40 O-linked glycans and 4-5 N-linked glycans. The central region of the G protein contains a 13-amino acid highly conserved domain, partially overlapping the cysteine noose domain with 4 cysteines linked 1-4 and 2-3, followed by a highly basic heparin-binding domain (HBD). The HBD is the likely attachment site for heparan sulfate (HS) found on the surface of most cells. A peptide from the G protein HBD (amino acids 184-198) binds efficiently to HEp-2 cells and inhibits RSV infection^[1].
The G protein is ~32 kDa without post-translational processing, ~95 kDa when fully glycosylated in Hep-2 cells, ~55 kDa cells after glycosylation and cleavage in Vero cells, and ~170 kDa after post-translational processing in primary human bronchial epithelial cells. G plays an important role in the first step of infection, binding to cell surface molecules through GAGs and/or CX3CR1. Second, G modulates host responses to infection which, in turn, affect immunity and disease. Third, the G-CX3CR1 interaction contributes to both binding to cells and modulating the host response to infection^[2].

Virus

HEK293

N-8*His

P20895 (H67-Q298)

Extracellular Domain

Approximately 90-110 kDa,based on SDS-PAGE under reducing conditions,due to the glycosylation.

Greater than 95% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.