RVFV G
(Rift Valley Fever Virus Glycoprotein (RVFV G))
Protein-Typ
Recombinant
Spezies
Rift Valley Fever Virus (RVFV)
Quelle
Baculovirus infected Insect Cells
Aufreinigungstag / Konjugat
Dieses RVFV G Protein ist gelabelt mit His tag.
Verwendungszweck
Recombinant Rift Valley fever virus (RVFV) (strain MP12) glycoprotein / G2 Protein (His Tag)
Sequenz
Cys691-Ser1139
Produktmerkmale
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.
Reinheit
> 90 as determined by SDS-PAGE.
Endotoxin-Niveau
< 1.0 EU per μg protein as determined by the LAL method.
Beschränkungen
Nur für Forschungszwecke einsetzbar
Format
Lyophilized
Rekonstitution
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.
Lagerung
4 °C,-20 °C,-80 °C
Informationen zur Lagerung
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))
Andere Bezeichnung
RVFV-G
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. 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.