Spike-forming protein that mediates virion attachment to the host epithelial cell receptors and plays a major role in cell penetration, determination of host range restriction and virulence. Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. It is subsequently lost, together with VP7, following virus entry into the host cell. Following entry into the host cell, low intracellular or intravesicular Ca(2+) concentration probably causes the calcium-stabilized VP7 trimers to dissociate from the virion. This step is probably necessary for the membrane-disrupting entry step and the release of VP4, which is locked onto the virion by VP7.; Forms the spike 'foot' and 'body' and acts as a membrane permeabilization protein that mediates release of viral particles from endosomal compartments into the cytoplasm. During entry, the part of VP5* that protrudes from the virus folds back on itself and reorganizes from a local dimer to a trimer. This reorganization may be linked to membrane penetration.; Forms the head of the spikes and mediates the recognition of specific host cell surface glycans. It is the viral hemagglutinin and an important target of neutralizing antibodies.
Pack Size | Availability | Price/USD | Quantity |
---|---|---|---|
20 μg | 20 days | $ 397.00 | |
100 μg | 20 days | $ 769.00 | |
500 μg | 20 days | $ 1,780.00 |
Description | Spike-forming protein that mediates virion attachment to the host epithelial cell receptors and plays a major role in cell penetration, determination of host range restriction and virulence. Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. It is subsequently lost, together with VP7, following virus entry into the host cell. Following entry into the host cell, low intracellular or intravesicular Ca(2+) concentration probably causes the calcium-stabilized VP7 trimers to dissociate from the virion. This step is probably necessary for the membrane-disrupting entry step and the release of VP4, which is locked onto the virion by VP7.; Forms the spike 'foot' and 'body' and acts as a membrane permeabilization protein that mediates release of viral particles from endosomal compartments into the cytoplasm. During entry, the part of VP5* that protrudes from the virus folds back on itself and reorganizes from a local dimer to a trimer. This reorganization may be linked to membrane penetration.; Forms the head of the spikes and mediates the recognition of specific host cell surface glycans. It is the viral hemagglutinin and an important target of neutralizing antibodies. |
Species | RVX |
Expression System | Yeast |
Tag | N-terminal 6xHis-tagged |
Accession Number | A9Q1L0 |
Amino Acid | MSLRSLLITTEAVGETTQTSDHQTSFSTRTYNEINDRPSLRVEKDGEKAYCFKNLDPVRYDTRMGEYPFDYGGQSTENNQLQFDLFTKDLMADTDIGLSDDVRDDLKRQIKEYYQQGYRAIFLIRPQNQEQQYIASYSSTNLNFTSQLSVGVNLSVLNKIQENKLHIYSTQPHIPSVGCEMITKIFRTDVDNENSLINYSVPVTVTISVTKATFEDTFVWNQNNDYPNMNYKDLIPAVTKNSIYHDVKR Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request. |
Construction | 1-249 aa |
Protein Purity | > 85% as determined by SDS-PAGE. |
Molecular Weight | 30.8 kDa as predicted |
Formulation | Tris-based buffer,50% glycerol |
Reconstitution | A hardcopy of COA with reconstitution instructions is sent along with the products. Please refer to it for detailed information. |
Stability & Storage |
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C. |
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. |
Research Background | Spike-forming protein that mediates virion attachment to the host epithelial cell receptors and plays a major role in cell penetration, determination of host range restriction and virulence. Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. It is subsequently lost, together with VP7, following virus entry into the host cell. Following entry into the host cell, low intracellular or intravesicular Ca(2+) concentration probably causes the calcium-stabilized VP7 trimers to dissociate from the virion. This step is probably necessary for the membrane-disrupting entry step and the release of VP4, which is locked onto the virion by VP7.; Forms the spike 'foot' and 'body' and acts as a membrane permeabilization protein that mediates release of viral particles from endosomal compartments into the cytoplasm. During entry, the part of VP5* that protrudes from the virus folds back on itself and reorganizes from a local dimer to a trimer. This reorganization may be linked to membrane penetration.; Forms the head of the spikes and mediates the recognition of specific host cell surface glycans. It is the viral hemagglutinin and an important target of neutralizing antibodies. |
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recombinant recombinant-proteins proteins protein