Recombinant Human Lipoprotein Lipase/LPL Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 9888-LL

R&D Systems, part of Bio-Techne
Catalog #
Availability
Size / Price
Qty
9888-LL-100
Print Quote
Bulk Order
100% Guarantee

Key Product Details

Source

CHO

Accession #

P06858

Conjugate

Unconjugated

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

Product Datasheets

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot number in the search box below.

Note: Certificate of Analysis not available for kit components.

Download SDS

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

For research use only

Privacy and Cookie Policy
Site Map
© Copyright 2024 Bio-Techne. All Rights Reserved.