Name :
Human respiratory syncytial virus (RSV) Fusion Protein (aa 1-526, His Tag)
Biological Activity :
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. The G protein mediates attachment of the virus to cell surface receptors, while the F protein promotes fusion of the viral and cellular membranes, allowing entry of the virus ribonucleoprotein into the cell cytoplasm. The fusion (F) protein of RSV is synthesized as a nonfusogenic precursor protein (F), which during its migration to the cell surface is activated by cleavage into the disulfide-linked F1 and F2 subunits. This fusion is pH independent and occurs directly at the outer cell membrane, and the F2 subunit was identifed as the major determinant of RSV host cell specificity. The trimer of F1-F2 interacts with glycoprotein G at the virion surface. Upon binding of G to heparan sulfate, the hydrophobic fusion peptide is unmasked and induces the fusion between host cell and virion membranes. Notably, RSV fusion protein is unique in that it is able to interact directly with heparan sulfate and therefore is sufficient for virus infection. Furthermore, the fusion protein is also able to trigger p53-dependent apoptosis.
Biological Activity :
Testing in progress
Expression Host :
RSV
Source :
Baculovirus-Insect Cells
Tag :
Protein Accession No. :
AHX57537.1
NCBI Gene ID :
Synonyms :
Synonyms :
Amino Acid Sequence :
Molecular Weight :
The recombinant Human respiratory syncytial virus (RSV) Fusion consists of 512 amino acids and predicts a molecular mass of 57.04 kDa.
Purity :
> 90% as determined by SDS-PAGE.
State of Matter :
Product Concentration :
Storage and Stability :
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Endotoxin Level :
< 1.0 EU per μg protein as determined by the LAL method.
Protein Construction :
A DNA sequence encoding the Human respiratory syncytial virus (RSV) Fusion (AHX57537.1) (Met1-Met526) was expressed with a polyhistidine tag at the C-terminus.
Buffer Solution :
Lyophilized from sterile 20mM PB, pH 7.5, 300mM NaCl, 10% glycerol.Please contact us for any concerns or special requirements. Normally 5 % – 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hardcopy of datasheet.
Shipping :
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.
Redissolution :
A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
Synonyms :
F Protein, RSV; HRSVgp08 Protein, RSV RSV Fusion 背景信息 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. The G protein mediates attachment of the virus to cell surface receptors, while the F protein promotes fusion of the viral and cellular membranes, allowing entry of the virus ribonucleoprotein into the cell cytoplasm. The fusion (F) protein of RSV is synthesized as a nonfusogenic precursor protein (F), which during its migration to the cell surface is activated by cleavage into the disulfide-linked F1 and F2 subunits. This fusion is pH independent and occurs directly at the outer cell membrane, and the F2 subunit was identifed as the major determinant of RSV host cell specificity. The trimer of F1-F2 interacts with glycoprotein G at the virion surface. Upon binding of G to heparan sulfate, the hydrophobic fusion peptide is unmasked and induces the fusion between host cell and virion membranes. Notably, RSV fusion protein is unique in that it is able to interact directly with heparan sulfate and therefore is sufficient for virus infection. Furthermore, the fusion protein is also able to trigger p53-dependent apoptosis.
References & Citations :
Martin-Gallardo A. et al., 1993, J Gen Virol. 74 (3): 453-8. Jose A M. et al., 1997, J Gen Virol. 78: 2411-8. Feldman SA. et al., 1999, J Virol. 73 (8): 6610-7. Zlateva K.T. et al., 2004, J Virol. 78 (9): 4675-83. Trento A. et al., 2006, J Virol. 80 (2): 975-84. Branigan P J. et al., 2006, J Gen Virol. 87 (2): 395-8. Eckardt-Michel J. et al., 2008, J. Virol. 82: 3236-49.
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