LASB Protein, Pseudomonas aeruginosa (P. pastoris, His)

LASB proteins are multifunctional enzymes that exhibit broad substrate specificity by cleaving host elastin, collagen, IgG, multiple complement components, and endogenous proaminopeptidases. Furthermore, LASB exhibits autocatalytic activity in processing its own propeptide and plays a role in processing the propeptide of chitin-binding protein (cbpD). LASB Protein, Pseudomonas aeruginosa (P. pastoris, His) is the recombinant LASB protein, expressed by P. pastoris , with N-6*His labeled tag. The total length of LASB Protein, Pseudomonas aeruginosa (P. pastoris, His) is 301 a.a., with molecular weight of 35.2 kDa.

LASB (LasA) protein, identified as a virulence factor in Pseudomonas aeruginosa, plays a significant role in the pathogenesis of infections. This calcium-dependent metalloprotease exhibits a broad substrate specificity, cleaving host elastin, collagen, IgG, and various complement components, along with endogenous pro-aminopeptidase. LASB engages in autocatalytic processing of its pro-peptide and also processes the pro-peptide of pro-chitin-binding protein (cbpD). These enzymatic activities contribute to the bacterium's virulence by facilitating tissue damage and immune evasion. The diverse substrate specificity and autocatalytic processing underscore LASB's multifaceted role in the pathogenicity of P. aeruginosa.

Others

P. pastoris

N-6*His

P14756 (A198-L498)

880368  [NCBI]

AEAGGPGGNQKIGKYTYGSDYGPLIVNDRCEMDDGNVITVDMNSSTDDSKTTPFRFACPTNTYKQVNGAYSPLNDAHFFGGVVFKLYRDWFGTSPLTHKLYMKVHYGRSVENAYWDGTAMLFGDGATMFYPLVSLDVAAHEVSHGFTEQNSGLIYRGQSGGMNEAFSDMAGEAAEFYMRGKNDFLIGYDIKKGSGALRYMDQPSRDGRSIDNASQYYNGIDVHHSSGVYNRAFYLLANSPGWDTRKAFEVFVDANRYYWTATSNYNSGACGVIRSAQNRNYSAADVTRAFSTVGVTCPSAL

35.2 kDa

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

<1 EU/μg, determined by LAL method.