Native Porcine Chymotrypsin-like Elastase 1 Pancreatic
| Catalog number: | B2017303 |
| Lot number: | Batch Dependent |
| Expiration Date: | Batch dependent |
| Amount: | 1000 U |
| Molecular Weight or Concentration: | N/A |
| Supplied as: | Powder |
| Applications: | a molecular tool for various biochemical applications |
| Storage: | 20C |
| Keywords: | pancreatic elastase I |
| Grade: | Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity>18 M-cm) and are filtered through 0.22 um. |
References
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- Wrtele M, Hahn M, Hilpert K, Hhne W. Atomic resolution structure of native porcine pancreatic elastase at 1.1 A Acta Crystallogr D Biol Crystallogr. 2000 Apr;56(Pt 4):520-3.
- Fu Z, Akula S, Thorpe M, Hellman L. Marked difference in efficiency of the digestive enzymes pepsin, trypsin, chymotrypsin, and pancreatic elastase to cleave tightly folded proteins Biol Chem. 2021 May 12;402(7):861-867.
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- Padrines M, Schneider-Pozzer M, Bieth JG. Inhibition of neutrophil elastase by alpha-1-proteinase inhibitor oxidized by activated neutrophils Am Rev Respir Dis. 1989 Mar;139(3):783-90.
- Ferreira GC, Bomediano Camillo LM, Sasaki SD. Structural and functional properties of rBmTI-A: A Kunitz-BPTI serine protease inhibitor with therapeutical potential Biochimie. 2023 Jan;204:1-7.








