Lipase Protein- Propionibacterium Acnes LIPASE Recombinant Protein from ProteoGenix; catalogue PX-P1121; research use only.
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Propionibacterium acnes lipase is a protein secreted by the Propionibacterium acnes which is a gram-positive anaerobic bacterium. This lipase protein metabolizes sebum which in turn results into metabolites that are responsible for the human skin condition known as acne vulgaris. It is also believed that lipase overexpression increases follicular development.
Propionibacterium acnes lipase protein acts on triglycerides to release free fatty acids. Among the fatty acids released, Palmitic acid stimulates the toll-like receptor 2-mediated inflammasome. The latter is associated with the release of interleukin-1, Th17 differenciation and interleukin-17-mediated keratinocyte proliferation. Oleic acid, another fatty acid released stimulates adhesion and keratinocyte proliferation in Propionibacterium acnes, also via the release of interleukin-1.
Antifugal drug ketoconazole has been suggested to inhibit P.acnes lipase activity. However, the mechanism by which ketoconazole inhibits P.acnes lipase protein remains unknown.
ProteoGenix catalogue number PX-P1121. For research use only.
Host: Escherichia coli (E.coli); Expression system: Prokaryotic expression; Purity: >95%; Molecular weight: 34,73 kDa; Tag: Yes; Fragment: Partial; Buffer: PBS pH7.5, DTT 1mM, 0.5mM Zwittergent 3-14 and 10% Glycerol if refolding. PBS, Urea 8M if denaturing conditions; Applications: ELISA, WB.
Available configurations: 50ug, 100ug, 1mg.
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