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Size | Qty | Add To Basket |
---|---|---|
100 μg | ||
1 mg |
Product Overview | Recombinant Avian infectious bronchitis virus (strain D3896) Spike glycoprotein (318-538 aa) was expressed in E. coli with a 6xHis-tag at the C-terminus. The biological activity was determined by its binding ability in a functional ELISA. This product can be used in ELISA, WB, IP. |
Source | E. coli |
Species | Avian infectious bronchitis virus (strain D3896) |
Fragment | 318-538 aa |
Sequence | ESDYMYGSYHPSCKFRLETINNGLWFNSLSVSLGYGPIQGGCKQSVFQNRATCCYAYSYNGPPLCKGVYRGELTKSFECGLLVFVTKTDGSRIQTRNEPFTLTQHNYNNITLDRCVEYNIYGRVGQGFITNVTNYAINYNYLADGGMAILDTSGAIDIFVVQGEYGLNYYKVNPCEDVNQQFVVSGGKLVGILTSRNETGSQPLENQFYIKIINGTRRSRR |
Tag | 6xHis-tag at the C-terminus |
Predicted MW | 25.8 kDa |
Purity | >90%, determined by SDS-PAGE. |
Conjugation | Unconjugated |
Target | S |
Full Name | Spike glycoprotein |
Uniprot ID | P17662 |
Background | 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. |
Alternate Names | S glycoprotein; E4; Peplomer protein; S |