Gastric Lipase Antibody (E-10): sc-390965

Gastric Lipase Antibody (E-10) is a mouse monoclonal IgG2b antibody that detects Gastric Lipase in human samples through various applications including western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), immunohistochemistry with paraffin-embedded sections (IHCP), and enzyme-linked immunosorbent assay (ELISA). Gastric Lipase is a 379-amino acid protein that plays a vital role in the digestion of dietary triglycerides, particularly in individuals with pancreatic lipase deficiencies. Secreted by the fundic mucosa of the stomach, this enzyme operates optimally under acidic pH conditions, where Gastric Lipase hydrolyzes the ester bonds of triglycerides, facilitating their breakdown into free fatty acids and glycerol. This process is crucial for proper nutrient absorption and energy metabolism, highlighting Gastric Lipase′s role in maintaining digestive health. Gastric Lipase′s ability to function effectively in the gastrointestinal tract underscores its significance in lipid metabolism and potential implications in various metabolic disorders. Gastric Lipase (E-10) antibody serves as an essential tool for researchers studying lipid digestion and related pathologies, providing reliable detection and characterization of this important protein.

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Gastric Lipase Antibody (E-10) References:

1. Establishment of culture systems of human gastric epithelium for the study of pepsinogen and gastric lipase synthesis and secretion.  |  Basque, JR. and Ménard, D. 2000. Microsc Res Tech. 48: 293-302. PMID: 10700046
2. Effects of lansoprazole on human gastric lipase secretion and intragastric lipolysis in healthy human volunteers.  |  Renou, C., et al. 2001. Digestion. 63: 207-13. PMID: 11435719
3. Characterization of fasted human gastric fluid for relevant rheological parameters and gastric lipase activities.  |  Pedersen, PB., et al. 2013. Eur J Pharm Biopharm. 85: 958-65. PMID: 23727368
4. Human gastric lipase. The N-terminal tetrapeptide is essential for lipid binding and lipase activity.  |  Bernbäck, S. and Bläckberg, L. 1989. Eur J Biochem. 182: 495-9. PMID: 2753032
5. Blocking Gastric Lipase Adsorption and Displacement Processes with Viscoelastic Biopolymer Adsorption Layers.  |  Scheuble, N., et al. 2016. Biomacromolecules. 17: 3328-3337. PMID: 27635994
6. Fatty acids generated by gastric lipase promote human milk triacylglycerol digestion by pancreatic colipase-dependent lipase.  |  Bernbäck, S., et al. 1989. Biochim Biophys Acta. 1001: 286-93. PMID: 2917153
7. Physico-chemical behaviors of human and bovine milk membrane extracts and their influence on gastric lipase adsorption.  |  Bourlieu, C., et al. 2020. Biochimie. 169: 95-105. PMID: 31866313
8. Human gastric lipase. Effects of fatty acid and bovine serum albumin on in vitro activity.  |  Kaminsky, S., et al. 1988. Scand J Clin Lab Invest. 48: 583-7. PMID: 3217760
9. Effect of sham feeding and acute suppression of acid secretion on human gastric lipase secretion.  |  Wøjdemann, M., et al. 1998. Am J Gastroenterol. 93: 244-8. PMID: 9468252
10. Inhibition of human gastric lipase secretion by glucagon-like peptide-1.  |  Wøjdemann, M., et al. 1998. Dig Dis Sci. 43: 799-805. PMID: 9558037

The preferred LAL antibody is LAL Antibody (9G7F12): sc-58374.