For researchers in the field of cell biology, CellSystems offers the full range of products for cell isolation and tissue dissociation. With the Worthington Biochemical Corporation enzymes and biochemicals you will maximize the yield of functionally viable, dissociated cells.
Pancreatic elastase is a serine protease with a specificity for peptide bonds adjacent to neutral amino acids
It also exhibits esterase and amidase activity. While elastase will hydrolyze a wide variety of protein substrates, it is unique among proteases in its ability to hydrolyze native elastin, a substrate not attacked by trypsin, chymotrypsin or pepsin. It is produced in the pancreas as an inactive zymogen, proelastase, and activated in the duodenum by trypsin. Elastase is also found in blood components and bacteria.
Because elastin is found in highest concentrations in the elastic fibers of connective tissues, elastase is frequently used to dissociate tissues which contain extensive intercellular fiber networks. For this purpose, it is usually used with other enzymes such as collagenase, trypsin, and chymotrypsin. Elastase is the enzyme of choice for the isolation of Type II cells from the lung.*
* Text is quoted from the Worthington Enzyme Manual.
|Elastase, Suspension||ES||≥3 units per mg protein||Porcine Pancreas|
|Elastase, Purified||ESFF||≥8 units per mg protein||Porcine Pancreas|
|Elastase, Lyophilized||ESL||≥3 units per mg protein||Porcine Pancreas|
|Collagenase/Elastase Vial (CLSH)||CLSH||≥ 22500 units collagense/ ≥30 units elastase per vial||Clostridium histolyticum/Porcine pancrease|