rh RSV-G is fused with a polyhistidine tag at the C-terminus, and has a calculated MW of 26.2 kDa. The predicted N-terminus is His 67. The reducing (R) protein migrates as 60-94 kDa in SDS-PAGE due to glycosylation.
Spezies: Human Herpesvirus 5 (HHV-5)
Wirt: HEK-293 Cells
Recombinant
>85 % as determined by SDS-PAGE.
WB
Beschränkungen
Nur für Forschungszwecke einsetzbar
Format
Lyophilized
Buffer
PBS, pH 7.4
Handhabung
Please avoid repeated freeze-thaw cycles.
Lagerung
-20 °C
Griffiths, Bilawchuk, McDonough, Jamieson, Elawar, Cen, Duan, Lin, Song, Casanova, Ogg, Jensen, Thienpont, Kumar, Hobman, Proud, Moraes, Marchant: "IGF1R is an entry receptor for respiratory syncytial virus." in: Nature, Vol. 583, Issue 7817, pp. 615-619, (2020) (PubMed).
Target
Glycoprotein / GP (Virus)
Substanzklasse
Viral Protein
Hintergrund
Human respiratory syncytial virus (HRSV) is the most common etiological agent of acute lower respiratory tract disease in infants and can cause repeated infections throughout life. Human respiratory syncytial virus A (strain Long) major surface glycoprotein G (RSV-G), a member of the pneumoviruses glycoprotein G family, is also known as attachment glycoprotein G and membrane-bound glycoprotein (mG), which contains a linear heparin binding domain essential for virus attachment to the host. Concretely speaking, RSV-G can attache the virion to the host cell membrane by interacting with heparan sulfate, initiating the infection. Furthermore, RSV-G can also interact with host CX3CR1, the receptor for the CX3C chemokine fractalkine, to modulate the immune response and facilitate infection. Unlike the other paramyxovirus attachment proteins, RSV-G lacks both neuraminidase and hemagglutinating activities.