| Description: | Alpha-hemolysin Protein engages with eukaryotic cell membranes, initiating low-molecular-weight molecule release and causing osmotic lysis. It inhibits host neutrophil chemotaxis to the lesion region. To exert lytic activity, heptamer oligomerization and pore formation are essential. Self-assembling, it forms a non-lytic oligomeric intermediate, adopting a mushroom-shaped homoheptamer structure up to 100 Angstroms in length and diameter. These structural features illuminate the intricate mechanisms by which Alpha-hemolysin interacts with cellular membranes, orchestrating processes leading to cell lysis and immune response modulation. Alpha-hemolysin Protein, S. aureus (P.pastoris, His) is the recombinant Staphylococcus aureus-derived Alpha-hemolysin protein, expressed by P. pastoris, with N-6*His labeled tag. The total length of Alpha-hemolysin Protein, S. aureus (P.pastoris, His) is 293 a.a., with molecular weight of ~35.3 kDa. |
