Recombinant Human Lipoprotein Lipase/LPL Protein, CF Summary
with a C-terminal 6-His tag
|Formulation||Supplied as a 0.2 μm filtered solution in Tris, NaCl, CHAPS and Glycerol.|
|Shipping||The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
- Assay Buffer: 50 mM Tris, pH 7.5
- Substrate Buffer: 50 mM Tris, 2% (v/v) Triton X-100, pH 7.5
- Recombinant Human LPL (rhLPL) (Catalog # 9888-LL)
- Substrate: 4-Nitrophenyl butyrate (Sigma, Catalog # N9876), 100 mM stock in acetone
- 96-well Clear Plate (Catalog # DY990)
- Plate Reader (Model: SpectraMax Plus by Molecular Devices) or equivalent
- Dilute rhLPL to 2 µg/mL in Assay Buffer.
- Load 100 µL of Assay Buffer to all wells.
- Add 50 μL of 2 µg/mL rhLPL to all wells.
- Dilute Substrate to 8 mM in Substrate Buffer.
- Add 50 μL of diluted Substrate to all wells. For Substrate Blank, load 150 μL of Assay Buffer followed by the addition of 50 μL of diluted Substrate.
- Read in kinetic mode for 5 minutes at an absorbance of 400 nm.
- Calculate specific activity:
Specific Activity (pmol/min/µg) =
|Adjusted Vmax* (OD/min) x Conversion Factor** (pmol/OD)|
|amount of enzyme (µg)|
*Adjusted for Substrate Blank.
**Derived using calibration standard 4-Nitrophenol (4-NP) (Sigma, Catalog # 241326).
Note: the output of many spectrophotometers is in mOD.
- rhLPL: 0.1 μg
- Substrate: 2 mM
Recombinant Human LPL activity can be inhibited byRecombinant Mouse ANGPTL3. Recombinant Mouse ANGPTL3 (Catalog # 9899-AN) dosedependently inhibits Recombinant Human LPL (Catalog # 9888-LL) activity with aND50 of 2‑10 µg/mL.
Recombinant Human Lipoprotein Lipase (Catalog # 9888-LL) is measured by its ability to hydrolyze 4-Nitrophenyl butyrate.
1 μg/lane of Recombinant Human Lipoprotein Lipase was resolved with SDS-PAGEunder reducing (R) and non-reducing (NR) conditions and visualized by silverstaining, showing a band at 60 kDa.
Background: Lipoprotein Lipase/LPL
Lipoprotein Lipase (LPL) is a rate-limiting enzyme responsible for the hydrolysis of triglycerides (1). LPL forms a non-covalent active homodimeric molecule (2). Monomeric LPL contains an N-terminal domain with the catalytic triad responsible for lipolysis and a 22-amino acid loop that serves as a cover for the catalytic site (3) in addition to a C-terminal domain that contains the region required for dimerization (4) as well as the primary heparin-binding domain that is important for lipoprotein binding. LPL is expressed in many tissues (5, 6) where it is synthesized in the ER of parenchymal cells and secreted to capillaries. LPL is highly controlled by regulatory factors such as apolipoproteins, angiopoietins, and hormones (7). LPL can be produced by macrophages and this expression is a critical event in the pathogenesis of atherosclerosis (8) in addition to contributing to the macrophage inflammatory response (9). Variants of LPL have been associated with altered risk of several diseases including coronary heart disease (10, 11), cerebrovascular accidents (12, 13) and Alzheimer's disease (14) and can result in LPL deficiency and consequent hyperlipidemia (15). LPL expression is a prognostic marker in B cell chronic lymphocytic leukemia (16) and has been linked to solid tumor cell proliferation (17). As LPL plays a critical role in several diseases, it is a therapeutic target for both inhibition (18) and induction (19). The LPL enzyme activity can be inhibited by Recombinant Mouse ANGPTL3.
- Wang, H. and R. H. Eckel (2009) Am. J. Physiol. Endocrinol. Metab. 297:E271.
- Olivecrona, T.G. et al. (1985) J. Biol. Chem. 260:6888.
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- Keiper, T. et al. (2001) J. Lipid Res. 42:1180.
- Camps, L. et al. (1991) J. Lipid Res. 32:1877.
- Savonen, R. et al. (2015) J. Lipid Res. 56:588.
- Ping-Ping, H. et al. (2018) Clin Chim Acta 480:126.
- Takahashi, M. et al. (2013) J. Lipid Res. 54:1124.
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- Gagne, S. E. et al. (1999) Clin. Genet. 55:450.
- Jensen, M. K. et al. (2009) Am. Heart J. 157:384.
- Wang, C. et al. (2011) Thromb. Res. 128:e107.
- Zhang, W. S. et al. (2015) Int. J. Clin. Exp. Med. 8:9575.
- Ren, L. and X. Ren (2016) Neurosci. Lett. 619:73.
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- Van Bockstaele, F. et al. (2007) Clin. Chem. 53:204.
- Kuemmerle, N.B. et al. (2011) Mol. Cancer Ther. 10:427.
- He, D. et al. (2016) J. Bioinform. Comput. Biol. 14:1650028.
- Takasu, S. et al. (2012) Biochem. Res. 2012:398697.
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