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NIV G Protein (His tag)

MALS verified NIV G Origin: Nipah Virus (NiV) Host: HEK-293 Cells Recombinant >95 % as determined by SDS-PAGE.
Catalog No. ABIN7121350
  • Target See all NIV G products
    NIV G (Nipah Virus Attachement protein (NIV G))
    Protein Type
    Recombinant
    Origin
    Nipah Virus (NiV)
    Source
    HEK-293 Cells
    Purification tag / Conjugate
    This NIV G protein is labelled with His tag.
    Purpose
    Nipah virus Glycoprotein, His Tag (MALS verified)
    Sequence
    Gln 71 - Thr 602
    Characteristics
    Nipah virus Glycoprotein, His Tag (GLN-N52H3) is expressed from human 293 cells (HEK293). It contains AA Gln 71 - Thr 602 (Accession # Q9IH62-1).
    Purity
    >95 % as determined by SDS-PAGE.
    Endotoxin Level
    Less than 1.0 EU per μg by the LAL method.
    Grade
    MALS verified
  • Application Notes
    This protein carries a polyhistidine tag at the N-terminus. The protein has a calculated MW of 61.2 kDa. The protein migrates as 70-100 kDa under reducing (R) condition due to glycosylation.
    Restrictions
    For Research Use only
  • Format
    Lyophilized
    Buffer
    PBS, pH 7.4
    Storage
    -20 °C
    Storage Comment
    -20°C
  • Target
    NIV G (Nipah Virus Attachement protein (NIV G))
    Alternative Name
    Nipah virus Glycoprotein (NIV G Products)
    Background
    Synonyms: Glycoprotein,
    Description: Hendra virus (HeV) and Nipah virus (NiV) are henipaviruses discovered in the mid-to late 1990s that possess a broad host tropism and are known to cause severe and often fatal disease in both humans and animals. HeV and NiV infect host cells through the coordinated efforts of two envelope glycoproteins. The G glycoprotein attaches to cell receptors, triggering the fusion (F) glycoprotein to execute membrane fusion. G is a type II homotetrameric transmembrane protein responsible for binding to ephrinB2 or ephrinB3 (ephrinB2/B3) receptors. F is a homotrimeric type I transmembrane protein that is synthesized as a premature F0 precursor and cleaved by cathepsin L during endocytic recycling to yield the mature, disulfide-linked, F1 and F2 subunits. Upon binding to ephrinB2/B3, NiV G undergoes conformational changes leading to F triggering and insertion of the F hydrophobic fusion peptide into the target membrane. Subsequent refolding into the more stable post-fusion F conformation drives merger of the viral and host membranes to form a pore for genome delivery to the cell cytoplasm.
    Molecular Weight
    61.2 kDa
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