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62335

Lipoprotein Lipase from Pseudomonas sp.

lyophilized, powder, ≥1200 U/mg

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About This Item

CAS Number:
9004-02-8
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-669-1
MDL number:
MFCD00131523
EC Number:
3.1.1.34 (BRENDA, IUBMB)
Specific activity:
≥1200 U/mg
Biological source:
bacterial (Pseudomonas spp.)

Key Documents

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biological source

bacterial (Pseudomonas spp.)

form

powder

quality

lyophilized

specific activity

≥1200 U/mg

storage temp.

−20°C

Quality Level

100

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This Item
L9656L951862309
Lipoprotein Lipase from Pseudomonas sp. lyophilized, powder, ≥1200 U/mg

Sigma-Aldrich

62335

Lipoprotein Lipase from Pseudomonas sp.

Lipoprotein Lipase from Burkholderia sp. lyophilized powder, ≥50,000 units/mg solid

Sigma-Aldrich

L9656

Lipoprotein Lipase from Burkholderia sp.

Lipase from Pseudomonas sp. Type XIII, lyophilized powder, ≥15 units/mg solid

Sigma-Aldrich

L9518

Lipase from Pseudomonas sp.

Lipase from Pseudomonas cepacia powder, light beige, ≥30 U/mg

Sigma-Aldrich

62309

Lipase from Pseudomonas cepacia

specific activity

≥1200 U/mg

specific activity

≥50,000 units/mg solid

specific activity

≥15 units/mg solid

specific activity

≥30 U/mg

biological source

bacterial (Pseudomonas spp.)

biological source

Burkholderia spp.

biological source

-

biological source

bacterial (Pseudomonas cepacia)

form

powder

form

lyophilized powder

form

lyophilized powder

form

powder

storage temp.

−20°C

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

2-8°C

Quality Level

100

Quality Level

200

Quality Level

200

Quality Level

100

quality

lyophilized

quality

-

quality

-

quality

-

Application

Lipoprotein Lipase from Pseudomonas sp. has been used in the enzymatic erosion studies in gamma irradiated poly(trimethylene carbonate) (PTMC) films.[1]

Biochem/physiol Actions

Lipoprotein lipase belongs to the family of triglyceride lipases.[2] It hydrolyses triglycerides in triglyceride-rich ApoB-containing lipoproteins.[3]
Malic dehydrogenase catalyzes the dehydrogenation of L-malate by NAD+.[4][5]

General description

Lipoprotein Lipase (LPL) is majorly secreted by myocytes and adipocytes in humans and is crucial for triglyceride homeostatis.[6] Mutations in the catalytic domain of LPL impairs its interaction with glycosylphosphatidylinositol anchored high density lipoprotein binding protein 1 (GPIHBP1).[7] 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.[8]

Other Notes

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)
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

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Certificates of Analysis (COA)

Lot/Batch Number
BCBH2863V
BCBQ3887V
BCBQ3888V

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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)
C.H. von der Osten et al.
Journal of the American Chemical Society, 111, 3924-3924 (1989)
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)
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)
G. Ottolina et al.
Biotechnology Letters, 14, 947-947 (1992)
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Protocols

LPL Activity Assay Protocol

Lipoprotein lipase (LPL) hydrolyzes triglycerides associated with VLDL.

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