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Lipoprotein lipase Antibody

Rabbit mAb

     
  •  - Lipoprotein lipase Antibody AP91289
    Western blot analysis of Lipoprotein lipase expression in Human fetal liver lysate.
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Product Information
Application
  • Applications Legend:
  • WB=Western Blot
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin-embedded Sections)
  • IHC-F=Immunohistochemistry (Frozen Sections)
  • IF=Immunofluorescence
  • FC=Flow Cytopmetry
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • E=ELISA
  • IP=Immunoprecipitation
  • DB=Dot Blot
  • CHIP=Chromatin Immunoprecipitation
  • FA=Fluorescence Assay
  • IEM=Immuno electron microscopy
  • EIA=Enzyme Immunoassay
WB, IHC
Primary Accession P06858
Clonality Monoclonal
Other Names HDLCQ11; LIPD; Lipoprotein lipase; LPL; LPL protein;
Isotype Rabbit IgG
Host Rabbit
Calculated MW 53162 Da
Additional Information
Dilution WB 1:1000~1:5000 IHC 1:50~1:200
Purification Affinity-chromatography
Immunogen A synthesized peptide derived from human Lipoprotein lipase
Description The primary function of this lipase is the hydrolysis of triglycerides of circulating chylomicrons and very low density lipoproteins (VLDL). Binding to heparin sulfate proteogylcans at the cell surface is vital to the function. The apolipoprotein, APOC2, acts as a coactivator of LPL activity in the presence of lipids on the luminal surface of vascular endothelium.
Storage Condition and Buffer Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at +4°C short term. Store at -20°C long term. Avoid freeze / thaw cycle.
Protein Information
Name LPL
Synonyms LIPD
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:11342582, PubMed:27578112, PubMed:8675619). Although it has both phospholipase and triglyceride lipase activities it is primarily a triglyceride lipase with low but detectable phospholipase activity (PubMed:12032167, PubMed:7592706). 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).
Cellular Location Cell membrane {ECO:0000250|UniProtKB:P11151}; Peripheral membrane protein {ECO:0000250|UniProtKB:P11151}; Extracellular side {ECO:0000250|UniProtKB:P11151}. Secreted. Secreted, extracellular space, extracellular matrix. Note=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) {ECO:0000250|UniProtKB:P11151, ECO:0000269|PubMed:27811232}
Tissue Location Detected in blood plasma (PubMed:11893776, PubMed:12641539, PubMed:2340307). Detected in milk (at protein level) (PubMed:2340307).
Research Areas
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$ 350.00
$ 175.00
Cat# AP91289
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