Recombinant Human Lipoprotein Lipase/LPL Protein, CF

Catalog # Availability Size / Price Qty
9888-LL-100
Lipoprotein Lipase/LPL Protein Enzyme Activity
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Recombinant Human Lipoprotein Lipase/LPL Protein, CF Summary

Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
Measured by its ability to hydrolyze 4-Nitrophenyl butyrate. The specific activity is >2,500 pmol/min/μg, as measured under the described conditions.
Source
Chinese Hamster Ovary cell line, CHO-derived human Lipoprotein Lipase/LPL protein
Ala28-Gly475
with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Analysis
Ala28
Predicted Molecular Mass
51 kDa
SDS-PAGE
55-64 kDa, reducing conditions

Product Datasheets

Data Images

Bioactivity Lipoprotein Lipase/LPL Protein Enzyme Activity View Larger

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.

Enzyme Activity Lipoprotein Lipase/LPL Protein Enzyme Activity View Larger

Recombinant Human Lipoprotein Lipase (Catalog # 9888-LL) is measured by its ability to hydrolyze 4-Nitrophenyl butyrate.

SDS-PAGE Lipoprotein Lipase/LPL Protein Enzyme Activity View Larger

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.

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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.

References
  1. Wang, H. and R. H. Eckel (2009) Am. J. Physiol. Endocrinol. Metab. 297:E271.
  2. Olivecrona, T.G. et al. (1985) J. Biol. Chem. 260:6888.
  3. Dugi, K. A. (1995) J. Biol. Chem. 270:25396.
  4. Keiper, T. et al. (2001) J. Lipid Res. 42:1180.
  5. Camps, L. et al. (1991) J. Lipid Res. 32:1877.
  6. Savonen, R. et al. (2015) J. Lipid Res. 56:588.
  7. Ping-Ping, H. et al. (2018) Clin Chim Acta 480:126.
  8. Takahashi, M. et al. (2013) J. Lipid Res. 54:1124.
  9. Qui, G. et al. (2007) J. Lipid Res. 48:385.
  10. Gagne, S. E. et al. (1999) Clin. Genet. 55:450.
  11. Jensen, M. K. et al. (2009) Am. Heart J. 157:384.
  12. Wang, C. et al. (2011) Thromb. Res. 128:e107.
  13. Zhang, W. S. et al. (2015) Int. J. Clin. Exp. Med. 8:9575.
  14. Ren, L. and X. Ren (2016) Neurosci. Lett. 619:73.
  15. Chan, L. Y. S. et al. (2002) Hum. Mutat. 20:232.
  16. Van Bockstaele, F. et al. (2007) Clin. Chem. 53:204.
  17. Kuemmerle, N.B. et al. (2011) Mol. Cancer Ther. 10:427.
  18. He, D. et al. (2016) J. Bioinform. Comput. Biol. 14:1650028.
  19. Takasu, S. et al. (2012) Biochem. Res. 2012:398697.
Entrez Gene IDs
4023 (Human); 16956 (Mouse); 24539 (Rat)
Alternate Names
EC 3.1.1; HDLCQ11; LIPD; LIPDEC 3.1.1.34; Lipoprotein Lipase; LPL

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