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MAK047
Lipase Activity Assay Kit II
sufficient for 100 colorimetric tests (with TNB standard)
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100 μL
CN¥5,551.31
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100 μL
CN¥5,551.31
About This Item
UNSPSC Code:
12161503
NACRES:
NA.84
Recommended Products
usage
sufficient for 100 colorimetric tests (with TNB standard)
detection method
colorimetric
relevant disease(s)
cancer; gastrointestinal diseases; pulmonary disorders
storage temp.
−20°C
1 of 4
This Item | HPA042634 | HPA043059 | HPA053160 |
|---|---|---|---|
| antibody form affinity isolated antibody | antibody form affinity isolated antibody | antibody form affinity isolated antibody | antibody form affinity isolated antibody |
| Quality Level 100 | Quality Level 100 | Quality Level 100 | Quality Level 100 |
| biological source rabbit | biological source rabbit | biological source rabbit | biological source rabbit |
| product line Prestige Antibodies® Powered by Atlas Antibodies | product line Prestige Antibodies® Powered by Atlas Antibodies | product line Prestige Antibodies® Powered by Atlas Antibodies | product line Prestige Antibodies® Powered by Atlas Antibodies |
| species reactivity human | species reactivity human | species reactivity human | species reactivity human |
General description
The lipase family of enzymes catalyze the cleavage of the ester bonds of lipids. In mammals, this family includes many critical members including pancreatic, hepatic, endothelial, and lipoprotein lipase. Lipases, such as pancreatic lipase, are critical for the metabolism of lipids. Lipases also play key roles in processes such as cell signaling and inflammation. Measurements of lipase activity are commonly used to screen for pancreatic injury or disease, and to monitor diseases such as cystic fibrosis, celiac disease, and Crohn′s disease.
Application
Lipase Activity Assay Kit II has been used to measure lipase activity.[1]
Features and Benefits
Compatible with high-throughput handling systems.
Suitability
Suitable for the detection of lipase activity in biological samples including tissue, cells and serum
Principle
The Lipase Activity Assay kit provides a simple and direct procedure for measuring lipase activity in a variety of samples. Lipase activity is determined using a coupled enzyme reaction, which results in a colorimetric (412 nm) product proportional to the enzymatic activity present. One unit of Lipase is the amount of enzyme that will generate 1.0 μmole of TNB per minute at 37 °C.
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Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Flam. Liq. 2 - Resp. Sens. 1
Storage Class Code
3 - Flammable liquids
Regulatory Information
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Inflammatory response of disc cells against Propionibacterium acnes depends on the presence of lumbar Modic changes.
Dudli S, et al.
European Spine Journal : Official Publication of the European Spine Society, the European Spinal Deformity Society, and the European Section of the Cervical Spine Research Society, 27(5), 1013-1020 (2018)
Stefan Dudli et al.
European spine journal : official publication of the European Spine Society, the European Spinal Deformity Society, and the European Section of the Cervical Spine Research Society, 27(5), 1013-1020 (2017-09-09)
Intervertebral disc with Propionibacterium acnes (P. acnes) is suggested to be an etiology of Modic type I changes in the adjacent bone marrow. However it is unknown if disc cells can respond to P. acnes and if bone marrow cells
Daniel Hernandez-Patlan et al.
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The three Bacillus strains present in Norum™ were initially selected by their excellent to good relative enzyme activity (REA) production score for amylase, protease, lipase, phytase, cellulase, β-glucanase, and xylanase. Further studies confirmed that the three isolates also showed an
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The aim of this experiment was to evaluate the effect of a phytogenic feed additive (PFA) on growth performance and nutrient digestibility of broilers fed corn and soybean meal-based diets containing two different levels of crude protein. A 2 ×
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In this study, hydrolytic and oxidative activities of enzymes isolated from halophilic microbes were characterized and applied for biomass utilization. First, lipase from Micrococcus luteus, and peroxidase and laccase from Pseudoalteromonas phenolica and Pseudoalteromonas peptidolytica were selected and their catalytic
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