Porcine Elastase
Native whole molecule, biologically active
Produktdetails
Synonyms
PPE, Pancreatopeptidase E
Description of Porcine Elastase
Elastase from porcine pancreas is a serine protease enzyme with a molecular weight of approximately 26 kDa, primarily responsible for hydrolyzing elastin—an essential protein in elastic fibers of connective tissue—as well as other substrates like hemoglobin, casein, and fibrin. It is synthesized in the pancreas and secreted into the intestine, where it breaks down dietary proteins during digestion. Elastase is unique among proteases for its ability to cleave native elastin, a property not shared by trypsin or chymotrypsin. Deficiency or dysfunction of pancreatic elastase is clinically significant, as it serves as a biomarker for exocrine pancreatic insufficiency (EPI), a condition marked by inadequate enzyme production leading to maldigestion, malabsorption, and symptoms such as steatorrhea, weight loss, and nutritional deficiencies. EPI is associated with diseases like chronic pancreatitis, cystic fibrosis, pancreatic cancer, diabetes, and celiac disease. In research and biotechnology, porcine pancreatic elastase is widely used for protein structural studies, tissue dissociation, and as a model enzyme in studies of extracellular matrix degradation and enzyme kinetics. Its robust activity and specificity make it valuable for in vitro assays and biomedical applications.
Source
Porcine pancreas was obtained from healthy animals of US origin and under the care of a registered veterinarian.
Biological Activity
> 50 units/mg protein Unit definition: One unit is defined as the amount of enzyme that will hydrolyze 1.0 umol of Suc-Ala-Ala-Pro-Abu-pNA per minute at 25ºC.
Storage
For long term, store Porcine Elastase at ≤ -20°C.
Applications
Cancer, Proteomics, In Vitro Diagnostics, Cancer, Diabetes, Cystic Fibrosis,.
Citations/Publications
Yang, F., et al., (2018), 'Manduca sexta serpin-12 controls the prophenoloxidase activation system in larval hemolymph', Insect Biochemistry and Molecular Biology 99: pp 27–36. Available at: https://doi.org/10.1016/j.ibmb.2018.05.004
Wang, Y., et al., (2020), 'Inhibition of immune pathway-initiating hemolymph protease-14 by Manduca sexta serpin-12, a conserved mechanism for the regulation of melanization and Toll activation in insects☆', Insect Biochemistry and Molecular Biology 116: pp 103261. Available at: https://doi.org/10.1016/j.ibmb.2019.103261
Chonzinski, T. J., et al., (2018), 'Volumetric, Nanoscale Optical Imaging of Mouse and Human Kidney via Expansion Microscopy', Scientific Reports. 8: pp 10396. Available at: DOI:10.1038/s41598-018-28694-2
NCBI: https://www.ncbi.nlm.nih.gov/protein/P00772
Shipped with ice packs
Gel Scan of Porcine Elastase
Fig. 1: SDS-PAGE Gel |
Usage: For research use only. Not for use in diagnostic or therapeutic procedures. Not for human use.
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Payment Methods
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