Specification
Organism | Avian infectious bronchitis virus (strain UK/123/82) (IBV) |
Expression Host | E.coli |
Tag Info | C-terminal 6xHis-tagged |
Purity | Greater than 85% by SDS-PAGE |
Uniprot ID | P30206 |
Gene Names | S |
Alternative Names | S glycoprotein;E2;Peplomer protein |
Expression Region | Partial(300-520aa ) |
Molecular Weight | 25.7 kDa |
Protein Sequence | ESDYMYGSYHPSCKFRLETINNGLSFNPLSVSLGYGPIQGGCKQSVFENRATCCYAYSYNGPPLCKGVYRGELTKSFECGLLVFVTKTDGSRIQTRNEPFTLTQHNYNNITLDRCVEYNIYGRVGQGFITNVTNYAINYNYLADGGMAILDTSGAIDIFVVQGEYGLNYYKVNPCEDVNQQFVVSGGKLVGILTSRNETGSQPLENQFYIKIINGTRRSRR |
Form | Liquid or Lyophilization |
Buffer | The default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol if the delivery form is liquid. The lyophilization buffer is Tris/PBS-based buffer, 6% Trehalose, pH 8.0 if the delivery form is lyophilized powder. Please contact us if you have any special requirment. |
Reconstitution | Please reconstitute protein in deionized sterile water and we recommend that briefly centrifuge thevial prior to opening the vial .We recommend aliquot for long-term storage at -20℃/-80℃. |
Background
Relevance | S1 attaches the virion to the cell membrane by interacting with cell receptors, initiating the infection. S2 is a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes (By similarity). |
Involvement in Disease | |
Subcellular Location | |
Protein Families | |
Tissue Specificity | S |
QC Data
Note | Please contact us for QC Data |
Product Image (Reference Only) | ![]() |