Outer Capsid Protein VP4, Recombinant, Rotavirus A, aa247-479, His-Tag

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 entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. According to the considered strain, VP4 seems to essentially target sialic acid and/or the integrin heterodimer ITGA2/ITGB1. Outer capsid protein VP5*: forms the spike "foot" and "body". Acts as a membrane permeabilization protein that mediates release of viral particles from endosomal compartments into the cytoplasm. In integrin-dependent strains, VP5* targets the integrin heterodimer ITGA2/ITGB1 for cell attachment. VP8* forms the head of the spikes. It is the viral hagglutinin and an important target of neutralizing antibodies. In sialic acid-dependent strains, VP8* binds to host cell sialic acid, most probably a ganglioside, providing the initial contact.

Source:
Recombinant protein corresponding to aa247-479 from rotavirus A Outer Capsid Protein VP4, fused to 6xHis-Tag at N-terminal, expressed in Yeast.

Molecular Weight:
~28.3kD

Amino Acid Sequence:
AQVSEDIIISKTSLWKEMQYNRDIIIRFKFNNSIIKLGGLGYKWSEISFKAANYQYNYLRDGEQVTAHTTCSVNGVNNFSYNGGLLPTHFSISRYEVIKENSYVYVDYWDDSQAFRNMVYVRSLAANLNSVKCSGGNYNFQMPVGAWPVMSGGAVSLHFAGVTLSTQFTDFVSLNSLRFRFSLTVEEPPFSILRTRVSGLYGLPASNPNSGHEYYEIAGRFSLISLVPSNDDY

Storage and Stability:
Lyophilized and reconstituted products are stable for 6 months after receipt at -20°C. Reconstitute with sterile ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.