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RVFV G Protein (His tag)

RVFV G Origin: Rift Valley Fever Virus (RVFV) Host: Baculovirus infected Insect Cells Recombinant > 90 as determined by SDS-PAGE.
Catalog No. ABIN7195956
  • Target
    RVFV G (Rift Valley Fever Virus Glycoprotein (RVFV G))
    Protein Type
    Recombinant
    Origin
    Rift Valley Fever Virus (RVFV)
    Source
    Baculovirus infected Insect Cells
    Purification tag / Conjugate
    This RVFV G protein is labelled with His tag.
    Purpose
    Recombinant Rift Valley fever virus (RVFV) (strain MP12) glycoprotein / G2 Protein (His Tag)
    Sequence
    Cys691-Ser1139
    Characteristics
    A DNA sequence encoding the Rift Valley fever virus (RVFV) (strain MP12) Gc (ABD38821.1) (Cys691-Ser1139) was expressed with a polyhistidine tag at the N-terminus.
    Purity
    > 90 as determined by SDS-PAGE.
    Endotoxin Level
    < 1.0 EU per μg protein as determined by the LAL method.
  • Restrictions
    For Research Use only
  • Format
    Lyophilized
    Reconstitution
    Please refer to the printed manual for detailed information.
    Buffer
    Lyophilized from sterile 20 mM Tris,150 mM NaCl, pH 8.0,10 % glycerol Normally 5 % - 8 % trehalose, mannitol and 0.01 % Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the printed manual.
    Storage
    4 °C,-20 °C,-80 °C
    Storage Comment
    Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
  • Target
    RVFV G (Rift Valley Fever Virus Glycoprotein (RVFV G))
    Alternative Name
    RVFV-G
    Target Type
    Viral Protein
    Background
    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. It is classified within the genus pneumovirus of the family paramyxoviridae. Like other members of the family, HRSV has two major surface glycoproteins (G and F) that play important roles in the initial stages of the infectious cycle. HRSV G protein is a type II glycoprotein of 289-299 amino acids (depending on the virus strain) with a signal/anchor hydrophobic domain and is extensively modified by the addition of both N-and O-linked oligosaccharides to achieve the mature form of 8-9 kDa. The C-terminal ectodomain of the G protein has a central region and four cysteines which are conserved in all HRSV isolates and have been proposed as the putative receptor binding site. The G protein mediates attachment of the virus to the host cell membrane by interacting with heparan sulfate, initiating the infection. As similar to mucins in amino acid compositions, the RSV G protein can interact with host CX3CR1, the receptor for the CX3C chemokine fractalkine, and thus modulates the immune response and facilitate infection. Secreted glycoprotein G helps RSV escape antibody-dependent restriction of replication by acting as an antigen decoy and by modulating the activity of leukocytes bearing Fcgamma receptors. Unlike the other paramyxovirus attachment proteins, HRSV-G lacks both neuraminidase and hemagglutinating activities.
    Molecular Weight
    50.1kDa.
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