Human Lipoprotein Lipase/LPL Antibody Summary
Ala28-Gly475
Accession # P06858
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
Lipoprotein Lipase/LPL in WM‑115 Human Cell Line. Lipoprotein Lipase/LPL was detected in immersion fixed WM‑115 human malignant melanoma cell line (positive staining) and MCF‑7 human breast cancer cell line (negative control) using Mouse Anti-Human Lipoprotein Lipase/LPL Monoclonal Antibody (Catalog # MAB7197) at 8 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Mouse IgG Secondary Antibody (red; NL007) and counterstained with DAPI (blue). Specific staining was localized to cytoplasm. Staining was performed using our protocol for Fluorescent ICC Staining of Non-adherent Cells.
Lipoprotein Lipase/LPL in Human Heart. Lipoprotein Lipase/LPL was detected in immersion fixed paraffin-embedded sections of human heart using Mouse Anti-Human Lipoprotein Lipase/LPL Monoclonal Antibody (Catalog # MAB7197) at 5 µg/mL for 1 hour at room temperature followed by incubation with the Anti-Mouse IgG VisUCyte™ HRP Polymer Antibody (VC001)). Before incubation with the primary antibody, tissue was subjected to heat-induced epitope retrieval using Antigen Retrieval Reagent-Basic (CTS013). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to cytoplasm in cardiomyocytes. Staining was performed our protocol for IHC Staining with VisUCyte HRP Polymer Detection Reagents.
Reconstitution Calculator
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
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.
- Dugi, K. A. (1995) J. Biol. Chem. 270:25396.
- 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.
- Qui, G. et al. (2007) J. Lipid Res. 48:385.
- 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.
- Chan, L. Y. S. et al. (2002) Hum. Mutat. 20:232.
- 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.
Product Datasheets
FAQs
No product specific FAQs exist for this product, however you may
View all Antibody FAQsReviews for Human Lipoprotein Lipase/LPL Antibody
There are currently no reviews for this product. Be the first to review Human Lipoprotein Lipase/LPL Antibody and earn rewards!
Have you used Human Lipoprotein Lipase/LPL Antibody?
Submit a review and receive an Amazon gift card.
$25/€18/£15/$25CAN/¥75 Yuan/¥2500 Yen for a review with an image
$10/€7/£6/$10 CAD/¥70 Yuan/¥1110 Yen for a review without an image