Gamma-hemolysin component B Protein, S. aureus (P.pastoris, His)

Gamma-hemolysin component B (HLgB) acts as a toxin, creating cell membrane pores with hemolytic and leukotoxic activities. Furthermore, HLgB promotes AMFR-mediated inflammation by promoting “Lys-27” linked ubiquitination of TAB3, mediating TAK1-TAB3 complex formation, and activating NF-kappa-B signaling. Gamma-hemolysin component B Protein, S. aureus (P.pastoris, His) is the recombinant Staphylococcus aureus-derived Gamma-hemolysin component B protein, expressed by P. pastoris , with N-His labeled tag. The total length of Gamma-hemolysin component B Protein, S. aureus (P.pastoris, His) is 300 a.a., with molecular weight of ~36.1 kDa.

Gamma-hemolysin component B (HlgB) functions as a toxin, exerting its effects by forming pores in the cell membrane and displaying hemolytic and leucotoxic activities. Additionally, HlgB plays a role in promoting host AMFR-mediated inflammation by facilitating 'Lys-27'-linked ubiquitination of TAB3, mediating TAK1-TAB3 complex formation, and phosphorylating TAK1/MAP3K7, thereby activating the host NF-kappa-B signaling pathway. The toxicity of HlgB relies on the sequential binding and synergistic association of a class S and a class F component, leading to the formation of heterooligomeric complexes. Specifically, HlgB (class F) associates either with HlgA, forming an AB toxin, or with HlgC, forming a CB toxin. These interactions and activities underscore the multifaceted nature of HlgB in cellular processes and host-pathogen interactions.

Staphylococcus aureus

P. pastoris

N-His

P0A075 (A26-K325)

59701249

AEGKITPVSVKKVDDKVTLYKTTATADSDKFKISQILTFNFIKDKSYDKDTLVLKATGNINSGFVKPNPNDYDFSKLYWGAKYNVSISSQSNDSVNVVDYAPKNQNEEFQVQNTLGYTFGGDISISNGLSGGLNGNTAFSETINYKQESYRTTLSRNTNYKNVGWGVEAHKIMNNGWGPYGRDSFHPTYGNELFLAGRQSSAYAGQNFIAQHQMPLLSRSNFNPEFLSVLSHRQDGAKKSKITVTYQREMDLYQIRWNGFYWAGANYKNFKTRTFKSTYEIDWENHKVKLLDTKETENNK

Approximately 36.1 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.