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Glycoprotein / GP (Virus) (AA 67-297) protein (His tag)

Origine: Human Respiratory Syncytial Virus (hRSV) Hôte: HEK-293 Cells Recombinant >90 % as determined by SDS-PAGE.
N° du produit ABIN2870785
  • Antigène
    Glycoprotein / GP (Virus)
    Type de proteíne
    Recombinant
    Attributs du protein
    AA 67-297
    Origine
    • 6
    • 3
    • 1
    • 1
    • 1
    Human Respiratory Syncytial Virus (hRSV)
    Source
    • 9
    HEK-293 Cells
    Purification/Conjugué
    His tag
    Séquence
    AA 67-297
    Attributs du produit
    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.
    Pureté
    >90 % as determined by SDS-PAGE.
    niveau d'endotoxine
    Less than 1.0 EU per μg by the LAL method.
  • Restrictions
    For Research Use only
  • Format
    Lyophilized
    Buffer
    PBS, pH 7.4
    Conseil sur la manipulation
    Please avoid repeated freeze-thaw cycles.
    Stock
    -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." dans: Nature, Vol. 583, Issue 7817, pp. 615-619, (2020) (PubMed).

  • Antigène
    Glycoprotein / GP (Virus)
    Classe de substances
    Viral Protein
    Sujet
    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.
    Poids moléculaire
    27.0 kDa
    UniProt
    P20895
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