| Description | 2-Naphthyl caprylateis a chromogenic substrate for CES (carboxylesterase) and lipase. 2-naphthol is released upon hydrolyzation. By simultaneous coupling with a diazonium salt, the corresponding azo-dye is formed. Naphthols can also be detected by fluorescence analysis. Used in an colorimetric assay2-Naphthyl caprylateis a chromogenic substrate for CES (carboxylesterase) and lipase. 2-naphthol is released upon hydrolyzation. By simultaneous coupling with a diazonium salt, the corresponding azo-dye is formed. Naphthols can also be detected by fluorescence analysis. Used in an colorimetric assay for the extracellular lipase of Pseudomonas fluorescens B52... Read More | Cardiolipin is a unique phospholipid present in the inner mitochondrial membrane, which makes up to 20% of total lipids. It is a non-bilayer anionic phospholipid, which has four acyl chains and small headgroupHeart CA has been used as a standard stock solution for its quantitative analysis using Cardiolipin is a unique phospholipid present in the inner mitochondrial membrane, which makes up to 20% of total lipids. It is a non-bilayer anionic phospholipid, which has four acyl chains and small headgroupHeart CA has been used as a standard stock solution for its quantitative analysis using liquid chromatography?mass spectrometry (LC-MS)/MS. It has also been used for liposome preparation... Read More | Inquire | Ganglioside GT1b is a brain ganglioside. It is composed of a neutral tetra-saccharide core, with one or two sialic acid on the internal galactose and an extra sialic acid on the non-reducing terminal of galactose | Trypsin is a pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains. It is derived from a 34 kDa inactive precursor zymogen, trypsinogen, after enzymatic removal of an N-terminal 6-amino acid leader sequence resulting in the 23.8 kDa Trypsin is a pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains. It is derived from a 34 kDa inactive precursor zymogen, trypsinogen, after enzymatic removal of an N-terminal 6-amino acid leader sequence resulting in the 23.8 kDa trypsin molecule. The optimum pH is 8.0. Trypsin is inhibited by organophosphorus compounds such as diisopropylfluorophosphate and natural inhibitors from pancreas. Soybean, lima bean, and egg white are also sources of natural inhibitors. Trypsin cleaves amide and ester bonds of Arg and Lys. The Aladdin Sequencing Grade Trypsin has been further purified to remove trace contaminating proteases and autolysis products which could interfere in trypsin digestion experiments, and exhibits a single band on PAGE.Trypsin is a serine protease used to hydrolyze proteins. Trypsin from bovine pancreas has a molecular weight of 23.8 kDa. Trypsins are used for the re-suspension of cells during cell culture and in proteomics research for the digestion of various proteins... Read More |