glycoprotein/G Protein, HRSV (258a.a, HEK293, His)

RSV G protein is a type II, highly glycosylated membrane protein with a full length of 292-319 amino acids (AA), an intracellular cytoplasmic tail (AA 1-37), and a transmembrane domain (AA 38 -66) and the extracellular domain ending in its carboxyl terminus.The RSV G protein has broad effects on the biology of RSV infection as well as host immune responses and infection-associated diseases.glycoprotein/G Protein, HRSV (HEK293, His) is the recombinant Virus-derived glycoprotein/G protein, expressed by HEK293 , with C-His labeled 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

C-His

AII22117 (S64-K321)

/

Approximately 29.59 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.