Human respiratory syncytial virus (RSV) (A, rsb1734) glycoprotein G / RSV-G Protein (93% Homology) (His Tag)

• 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.

• Synonyms:

  G Protein, RSV

• UniProt:

  P27022-1

• Expression System:

  Baculovirus-Insect Cells

• Tag:

  C-His

• Endotoxin:

  < 1.0 EU per μg of the protein as determined by the LAL method.

• Purity:

  > 92 % as determined by SDS-PAGE.

• Activity:

  At Leading Biology, the biological activity of a recombinant protein is routinely measured using a bioassay, e.g. chemotaxis or cell proliferation assay, enzyme assay, or a functional ELISA. When a recombinant protein is an enzyme, specific activity is derived from an enzymatic assay. Each enzyme is tested for potency by cleavage of a substrate. We are in the process of updating the biological activity data. If you have any questions regarding this update, please feel free to contact our technical support team.

• Form:

  Lyophilized

• Buffer:

  Lyophilized from sterile 50mM Tris, 100mM NaCl, pH 8.0, 10% glycerol, 0.5mM EDTA, 0.5mM PMSF Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.

• Function:

  RSV, Viral Proteins, Human Respiratory Syncytial Virus A

• Molecular Weight:

  The secreted recombinant human RSV-G comprises 242 amino acids and has a predicted molecular mass of 26.3 kDa. As a result of glycosylation, the apparent molecular mass of RSV protein G is approximately 40-55 kDa in SDS-PAGE under reducing conditions.

• Storage Conditions:

  In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise. Stable for 1 year at -20°C or below from date of shipment. For maximum recovery of product, centrifuge the original vial after thawing and opening the cap. For long-term storage, aliquot and store at -20°C or below. Avoid repeated freeze-thaw cycles.

• Symbol:

  RSV-G

• Species:

  RSV

• Overview:

  A DNA sequence encoding the glycoprotein G extracellular domain (Asn 66-Arg297) of human respiratory syncytial virus A (93% homologous with strain rsb1734) (P27022-1) was expressed, with a C-terminal polyhistidine tag.

• Uniprot URL:

  https://www.uniprot.org/uniprot/P27022-1

• AA Sequence:

  Asn66-Arg297