protein

Lanosterol synthase/LSS Protein, Human (P.pastoris, His)

HY-P72309

2 μg;10 μg;50 μg

70;175;480 USD

Lanosterol synthase/LSS Protein, Human (P.pastoris, His)

proteins

P. pastoris

2 μg;10 μg;50 μg

70;175;480 USD

LSS protein, a pivotal enzyme in cholesterol biosynthesis, catalyzes the cyclization of (S)-2,3 oxidosqualene into lanosterol, a crucial step in sterol nucleus formation. Beyond cholesterol biosynthesis, LSS may regulate lens protein aggregation, maintaining lens transparency. LSS's enzymatic action impacts fundamental and specialized cellular processes, underscoring its significance in diverse physiological contexts. Lanosterol synthase/LSS Protein, Human (P.pastoris, His) is the recombinant human-derived Lanosterol synthase/LSS protein, expressed by P. pastoris , with N-His labeled tag. The total length of Lanosterol synthase/LSS Protein, Human (P.pastoris, His) is 731 a.a., with molecular weight of ~86.0 kDa.

Human

Lanosterol synthase (LSS) emerges as a pivotal enzyme in the cholesterol biosynthesis pathway, orchestrating the cyclization of (S)-2,3 oxidosqualene into lanosterol. This catalytic activity holds a key role in the formation of the sterol nucleus, a critical step in cholesterol production. Beyond its role in cholesterol biosynthesis, LSS has been implicated in potential regulatory functions related to lens protein aggregation, suggesting a role in maintaining lens transparency. The enzymatic action of LSS not only contributes to fundamental cellular processes but may also extend its impact to specialized functions, highlighting its significance in cellular and physiological contexts.

OSCLanosterol synthase; Oxidosqualene--lanosterol cyclase; OSC

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

Lyophilized from 0.22 μm filtered solution in PBS, pH 7.4.

Room temperature in continental US; may vary elsewhere.