62335
Lipoprotein Lipase from Pseudomonas sp.
lyophilized, powder, ≥1200 U/mg
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About This Item
Recommended Products
biological source
bacterial (Pseudomonas spp.)
Quality Level
form
powder
quality
lyophilized
specific activity
≥1200 U/mg
storage temp.
−20°C
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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.
Application
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
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Journal of Lipid Research, jlr-M070813 (2016)
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)
G. Ottolina et al.
Biotechnology Letters, 14, 947-947 (1992)
Lipoprotein lipase: biosynthesis, regulatory factors, and its role in atherosclerosis and other diseases
He PP, et al.
Clinica Chimica Acta; International Journal of Clinical Chemistry, 480, 126-137 (2018)
Protocols
Lipoprotein lipase (LPL) hydrolyzes triglycerides associated with VLDL.
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