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Mouse Anti-LPL Recombinant Antibody (CBYJL-1931) (CBMAB-L1981-YJ)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
CBYJL-1931
Antibody Isotype
IgG1
Application
WB, IHC-P

Basic Information

Specificity
Human
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Buffer
PBS, pH 7.4
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
LPL
Introduction
LPL is expressed in heart, muscle, and adipose tissue. LPL functions as a homodimer, and has the dual functions of triglyceride hydrolase and ligand/bridging factor for receptor-mediated lipoprotein uptake. Severe mutations that cause LPL deficiency result in type I hyperlipoproteinemia, while less extreme mutations in LPL are linked to many disorders of lipoprotein metabolism.
Entrez Gene ID
4023
UniProt ID
P06858
Alternative Names
LIPD; HDLCQ11; lipoprotein lipase; EC 3.1.1.34
Function
Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage (PubMed:8675619, PubMed:11342582, PubMed:27578112).
Although it has both phospholipase and triglyceride lipase activities it is primarily a triglyceride lipase with low but detectable phospholipase activity (PubMed:7592706, PubMed:12032167).
Mediates margination of triglyceride-rich lipoprotein particles in capillaries (PubMed:24726386).
Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans (PubMed:11342582, PubMed:27811232).
Biological Process
Cellular response to fatty acidISS:ARUK-UCL
Cellular response to nutrientISS:ARUK-UCL
Cholesterol homeostasisManual Assertion Based On ExperimentIMP:BHF-UCL
Chylomicron remodelingManual Assertion Based On ExperimentIMP:UniProtKB
Fatty acid biosynthetic processManual Assertion Based On ExperimentIDA:BHF-UCL
Fatty acid metabolic processManual Assertion Based On ExperimentIDA:UniProtKB
Lipid catabolic processManual Assertion Based On ExperimentIBA:GO_Central
Low-density lipoprotein particle mediated signalingManual Assertion Based On ExperimentIMP:BHF-UCL
Negative regulation of cellular response to insulin stimulusIEA:Ensembl
Phospholipid metabolic processBy SimilarityISS:BHF-UCL
Positive regulation of chemokine (C-X-C motif) ligand 2 productionISS:ARUK-UCL
Positive regulation of chemokine productionManual Assertion Based On ExperimentIMP:BHF-UCL
Positive regulation of cholesterol storageManual Assertion Based On ExperimentIMP:BHF-UCL
Positive regulation of fat cell differentiationManual Assertion Based On ExperimentIMP:ARUK-UCL
Positive regulation of inflammatory responseISS:ARUK-UCL
Positive regulation of interleukin-1 beta productionISS:ARUK-UCL
Positive regulation of interleukin-6 productionISS:ARUK-UCL
Positive regulation of lipid storageManual Assertion Based On ExperimentTAS:ARUK-UCL
Positive regulation of macrophage derived foam cell differentiation1 PublicationIC:BHF-UCL
Positive regulation of sequestering of triglycerideManual Assertion Based On ExperimentIMP:BHF-UCL
Positive regulation of tumor necrosis factor productionISS:ARUK-UCL
Response to bacteriumIEA:Ensembl
Response to coldIEA:Ensembl
Response to glucoseISS:AgBase
Response to xenobiotic stimulusIEA:Ensembl
Triglyceride biosynthetic processIEA:Ensembl
Triglyceride catabolic processManual Assertion Based On ExperimentIDA:UniProtKB
Triglyceride homeostasisManual Assertion Based On ExperimentIGI:BHF-UCL
Triglyceride metabolic processBy SimilarityISS:BHF-UCL
Very-low-density lipoprotein particle remodelingManual Assertion Based On ExperimentIDA:BHF-UCL
Cellular Location
Cell membrane
Secreted
Secreted, extracellular space, extracellular matrix
Newly synthesized LPL binds to cell surface heparan proteoglycans and is then released by heparanase. Subsequently, it becomes attached to heparan proteoglycan on endothelial cells (PubMed:27811232).
Locates to the plasma membrane of microvilli of hepatocytes with triglyceride-rich lipoproteins (TRL). Some of the bound LPL is then internalized and located inside non-coated endocytic vesicles (By similarity).
Involvement in disease
Hyperlipoproteinemia 1 (HLPP1):
An autosomal recessive metabolic disorder characterized by defective breakdown of dietary fats, impaired clearance of chylomicrons from plasma causing the plasma to have a milky appearance, and severe hypertriglyceridemia. On a normal diet, patients often present with abdominal pain, hepatosplenomegaly, lipemia retinalis, eruptive xanthomata, and massive hypertriglyceridemia, sometimes complicated with acute pancreatitis.
Hyperlipidemia, familial combined, 3 (FCHL3):
A disorder characterized by a variable pattern of elevated levels of serum total cholesterol, triglycerides or both. It is observed in a percentage of individuals with premature coronary heart disease. FCHL3 inheritance is autosomal dominant.
PTM
Tyrosine nitration after lipopolysaccharide (LPS) challenge down-regulates the lipase activity.
More Infomation

Pirahanchi, Y., Anoruo, M., & Sharma, S. (2022). Biochemistry, lipoprotein lipase. StatPearls [Internet].

Shang, R., & Rodrigues, B. (2021). Lipoprotein lipase and its delivery of fatty acids to the heart. Biomolecules, 11(7), 1016.

Kumari, A., Kristensen, K. K., Ploug, M., & Winther, A. M. L. (2021). The importance of lipoprotein lipase regulation in atherosclerosis. Biomedicines, 9(7), 782.

Wu, S. A., Kersten, S., & Qi, L. (2021). Lipoprotein lipase and its regulators: an unfolding story. Trends in Endocrinology & Metabolism, 32(1), 48-61.

Kuthiroly, S., Yesodharan, D., Radhakrishnan, N., Ganapathy, A., Mannan, A. U., Hoffmann, M. M., & Nampoothiri, S. (2021). Lipoprotein lipase deficiency. The Indian Journal of Pediatrics, 88, 147-153.

Basu, D., & Goldberg, I. J. (2020). Regulation of lipoprotein lipase-mediated lipolysis of triglycerides. Current opinion in lipidology, 31(3), 154.

Chang, H. R., Josefs, T., Scerbo, D., Gumaste, N., Hu, Y., Huggins, L. A., ... & Goldberg, I. J. (2019). Role of LpL (lipoprotein lipase) in macrophage polarization in vitro and in vivo. Arteriosclerosis, thrombosis, and vascular biology, 39(10), 1967-1985.

Beigneux, A. P., Allan, C. M., Sandoval, N. P., Cho, G. W., Heizer, P. J., Jung, R. S., ... & Young, S. G. (2019). Lipoprotein lipase is active as a monomer. Proceedings of the National Academy of Sciences, 116(13), 6319-6328.

Arora, R., Nimonkar, A. V., Baird, D., Wang, C., Chiu, C. H., Horton, P. A., ... & Trauger, J. W. (2019). Structure of lipoprotein lipase in complex with GPIHBP1. Proceedings of the National Academy of Sciences, 116(21), 10360-10365.

Gutgsell, A. R., Ghodge, S. V., Bowers, A. A., & Neher, S. B. (2019). Mapping the sites of the lipoprotein lipase (LPL)–angiopoietin-like protein 4 (ANGPTL4) interaction provides mechanistic insight into LPL inhibition. Journal of Biological Chemistry, 294(8), 2678-5366.

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For research use only. Not intended for any clinical use.

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