Recombinant Human Lipoprotein Lipase/LPL Protein, CF

R&D Systems | Catalog # 9888-LL

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Key Product Details

  • R&D Systems CHO-derived Recombinant Human Lipoprotein Lipase/LPL Protein (9888-LL)
  • Quality control testing to verify active proteins with lot specific assays by in-house scientists
  • All R&D Systems proteins are covered with a 100% guarantee

Source

CHO

Accession Number

P06858

Applications

Enzyme Activity
View all Lipoprotein Lipase/LPL Proteins and Enzymes »

Product Specifications

Source

Chinese Hamster Ovary cell line, CHO-derived human Lipoprotein Lipase/LPL protein
Ala28-Gly475 with a C-terminal 6-His tag

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Ala28

Predicted Molecular Mass

51 kDa

SDS-PAGE

55-64 kDa, reducing conditions

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.

Scientific Data Images for Recombinant Human Lipoprotein Lipase/LPL Protein, CF

Recombinant Human Lipoprotein Lipase/LPL Protein Bioactivity

Recombinant Human Lipoprotein Lipase/LPL Protein Bioactivity

Recombinant Human LPL activity can be inhibited by Recombinant Mouse ANGPTL3. Recombinant Mouse ANGPTL3 (Catalog # 9899-AN) dose dependently inhibits Recombinant Human LPL (Catalog # 9888-LL) activity with a ND50of 2-10 µg/mL.
Recombinant Human Lipoprotein Lipase/LPL Protein Enzyme Activity

Recombinant Human Lipoprotein Lipase/LPL Protein Enzyme Activity

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

Recombinant Human Lipoprotein Lipase/LPL Protein SDS-PAGE

1 μg/lane of Recombinant Human Lipoprotein Lipase was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by silver staining, showing a band at 60 kDa.

Formulation, Preparation, and Storage

9888-LL
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.
  • 6 months from date of receipt, -70 °C as supplied.
  • 3 months, -70 °C under sterile conditions after opening.

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.

Alternate Names

LIPD, LPL

Entrez Gene IDs

4023 (Human); 16956 (Mouse); 24539 (Rat)

Gene Symbol

LPL

UniProt

P06858 (Human)

Additional Lipoprotein Lipase/LPL Products

Product Documents for Recombinant Human Lipoprotein Lipase/LPL Protein, CF

Certificate of Analysis

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Product Specific Notices for Recombinant Human Lipoprotein Lipase/LPL Protein, CF

For research use only

Citations for Recombinant Human Lipoprotein Lipase/LPL Protein, CF

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Protocols

View specific protocols for Recombinant Human Lipoprotein Lipase/LPL Protein, CF (9888-LL):

Materials
  • 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
  1. Dilute rhLPL to 2 µg/mL in Assay Buffer.
  2. Load 100 µL of Assay Buffer to all wells.
  3. Add 50 μL of 2 µg/mL rhLPL to all wells.
  4. Dilute Substrate to 8 mM in Substrate Buffer.
  5. 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.
  6. Read in kinetic mode for 5 minutes at an absorbance of 400 nm.
  7. 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.

Per Well:

  • rhLPL: 0.1 μg
  • Substrate: 2 mM

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