Lipoprotein Lipase from Pseudomonas sp.

lyophilized, powder, ≥1200 U/mg

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
Pricing and availability is not currently available.



Quality Level



specific activity

≥1200 U/mg

storage temp.


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General description

Lipoprotein Lipase (LPL) is majorly secreted by myocytes and adipocytes in humans and is crucial for triglyceride homeostatis. Mutations in the catalytic domain of LPL impairs its interaction with glycosylphosphatidylinositol anchored high density lipoprotein binding protein 1 (GPIHBP1). The N-terminal catalytic domain is essential for lipolysis. The C-terminal is crucial for binding lipoproteins. Altered LPL levels may play role in the pathogenesis of atherosclerosis, coronary heart disease and chronic lymphocytic leukemia.


Lipoprotein Lipase from Pseudomonas sp. has been used in the enzymatic erosion studies in gamma irradiated poly(trimethylene carbonate) (PTMC) films.

Biochem/physiol Actions

Malic dehydrogenase catalyzes the dehydrogenation of L-malate by NAD+.
Lipoprotein lipase belongs to the family of triglyceride lipases. It hydrolyses triglycerides in triglyceride-rich ApoB-containing lipoproteins.

Unit Definition

1 U corresponds to the amount of enzyme which liberates 1 μmol oleic acid per minute at pH 8.0 and 40°C (triolein, Cat. No. 62314 as substrate)

Other Notes

Preparation of aldol acceptors (R)- and (S)-3-azido-2-hydroxypropanal via lipase-catalyzed resolution of the racemic acetal precursor; Effect of enzyme form on its properties in toluene

Personal Protective Equipment

dust mask type N95 (US),Eyeshields,Gloves


NONH for all modes of transport

WGK Germany


Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis
Certificate of Origin
A lipoprotein lipase (LPL)-specific monoclonal antibody, 88B8, that abolishes the binding of LPL to GPIHBP1
Allan CM, et al.
Journal of Lipid Research, jlr-M070813 (2016)
Macrophage-mediated erosion of gamma irradiated poly (trimethylene carbonate) films
Bat E, et al.
Biomaterials, 30(22), 3652-3661 (2009)
G. Ottolina et al.
Biotechnology Letters, 14, 947-947 (1992)
C.H. von der Osten et al.
Journal of the American Chemical Society, 111, 3924-3924 (1989)
Mutations in lipoprotein lipase that block binding to the endothelial cell transporter GPIHBP1
Voss CV, et al.
Proceedings of the National Academy of Sciences of the USA, 108(19), 7980-7984 (2011)
Lipoprotein lipase (LPL) hydrolyzes triglycerides associated with VLDL.
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