LIPASE SUBSTRATE CHROMOGENIC
LIPASE SUBSTRATE CHROMOGENIC structure
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Common Name | LIPASE SUBSTRATE CHROMOGENIC | ||
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| CAS Number | 195833-46-6 | Molecular Weight | 752.031 | |
| Density | 1.1±0.1 g/cm3 | Boiling Point | 792.2±60.0 °C at 760 mmHg | |
| Molecular Formula | C45H69NO8 | Melting Point | 29 - 31°C (lit.) | |
| MSDS | Chinese USA | Flash Point | 151.3±27.3 °C | |
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Modulation of the Activity of Mycobacterium tuberculosis LipY by Its PE Domain.
PLoS ONE 10 , e0135447, (2015) Mycobacterium tuberculosis harbors over 160 genes encoding PE/PPE proteins, several of which have roles in the pathogen's virulence. A number of PE/PPE proteins are secreted via Type VII secretion systems known as the ESX secretion systems. One PE protein, Li... |
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A Novel Aqueous Two Phase System Composed of Surfactant and Xylitol for the Purification of Lipase from Pumpkin (Cucurbita moschata) Seeds and Recycling of Phase Components.
Molecules 20 , 11184-201, (2015) Lipase is one of the more important enzymes used in various industries such as the food, detergent, pharmaceutical, textile, and pulp and paper sectors. A novel aqueous two-phase system composed of surfactant and xylitol was employed for the first time to pur... |
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A new fluorescence method for the continuous determination of surface lipid oxidation in lipoproteins and plasma.
Free Radic. Res. 23(4) , 317-27, (1995) We report on a new method for the determination of lipid oxidation in lipoproteins and plasma. The biological lipid system is preloaded with a fluorescent analog of phosphatidylcholine containing diphenylhexatriene (DPH) propionic acid covalently linked to th... |
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Novel fluorescent phosphonic acid esters for discrimination of lipases and esterases.
ChemBioChem. 6(10) , 1776-81, (2005) Lipases and esterases are responsible for carboxylester hydrolysis inside and outside cells and are useful biocatalysts for (stereo)selective modification of synthetic substrates. Here we describe novel fluorescent suicide inhibitors that differ in structure ... |
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Activity-based proteomics: enzymatic activity profiling in complex proteomes.
Amino Acids 30(4) , 333-50, (2006) In the postgenomic era new technologies are emerging for global analysis of protein function. The introduction of active site-directed chemical probes for enzymatic activity profiling in complex mixtures, known as activity-based proteomics has greatly acceler... |
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Inhibitor and protein microarrays for activity-based recognition of lipolytic enzymes.
ChemBioChem. 7(3) , 527-34, (2006) Protein and small-molecule microarrays are useful tools for high-throughput analysis of DNA-protein, protein-protein, and protein-small molecule interactions. Here we report on novel microarrays for activity screening of lipases and esterases based on phospho... |
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Fluorescent inhibitors for the qualitative and quantitative analysis of lipolytic enzymes.
Anal. Biochem. 276(1) , 72-80, (1999) We report on the determination of active enzyme components in pure and crude lipases, using fluorescent inhibitors for covalent modification and visualization of the enzymatically active proteins. Lipase-specific compounds are triacylglycerol analogs, namely ... |
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Mapping the lipolytic proteome of adipose tissue using fluorescent suicide inhibitors.
Methods Mol. Biol. 579 , 497-511, (2009) Lipases are responsible for the hydrolysis of acylglycerols and cholesteryl esters in animals, plants, and microorganisms. In this chapter we describe a tool for the concomitant analysis of lipases in complex proteomes. For this purpose, the target enzymes ar... |
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Simplified assays of lipolysis enzymes for drug discovery and specificity assessment of known inhibitors.
J. Lipid Res. 57 , 131-41, (2016) Lipids are used as cellular building blocks and condensed energy stores and also act as signaling molecules. The glycerolipid/ fatty acid cycle, encompassing lipolysis and lipogenesis, generates many lipid signals. Reliable procedures are not available for me... |
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Evidence for Two Distinct Binding Sites for Lipoprotein Lipase on Glycosylphosphatidylinositol-anchored High Density Lipoprotein-binding Protein 1 (GPIHBP1).
J. Biol. Chem. 290 , 13919-34, (2015) GPIHBP1 is an endothelial membrane protein that transports lipoprotein lipase (LPL) from the subendothelial space to the luminal side of the capillary endothelium. Here, we provide evidence that two regions of GPIHBP1, the acidic N-terminal domain and the cen... |