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Sigma-Aldrich

Elastase from porcine pancreas

lyophilized, powder, white, ~8 U/mg

Synonym(s):

Elastase from hog pancreas, Pancreatopeptidase E

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204

biological source

Porcine pancreas

form

powder

quality

lyophilized

specific activity

~8 U/mg

mol wt

Mr ~25000

impurities

salt, none detected

color

white

storage temp.

−20°C

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Biochem/physiol Actions

Elastase hydrolyses elastin, the specific protein of elastic fibers, and digests hemoglobin, casein and fibrin.

Unit Definition

1 U corresponds to the amount of enzyme which liberates 1 μmol 4-nitroaniline per minute at 25°C and pH 7.8 (succinyl-(L-Ala)3-4-nitroanilide as substrate)
One unit will hydrolyze 1.0 μmole of N-succinyl-L-Ala-Ala-Ala-p-nitroanilide per min, pH 8.0 at 25 °C.

Other Notes

For protein sequence studies, limited proteolysis; Application in (selective) hydrolysis/condensation of carboxylic ester bonds
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Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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I Grunnet et al.
The Biochemical journal, 209(1), 215-222 (1983-01-01)
Fatty acid synthetase from goat mammary gland was subjected to limited proteolysis by trypsin and elastase. Both proteolytic enzymes selectively cleaved the chain-terminating thioester hydrolase component from the enzyme complex, leaving all other partial activities intact in the core peptides.
T. Sakurai et al.
Journal of the American Chemical Society, 110, 7236-7236 (1988)
Ping-Chung Kuo et al.
Journal of natural products, 76(2), 230-236 (2013-01-26)
Phytochemical investigation of the methanolic extract of Croton tonkinensis afforded two known kauranes (1, 2), eight new ent-kauranes (3-10), and 16 known ent-kaurane-type diterpenoids (12-27). In addition, 30 known compounds were identified by comparison of their physical and spectroscopic data
Lilibeth A Salvador et al.
Journal of medicinal chemistry, 56(3), 1276-1290 (2013-01-29)
We discovered new structural diversity to a prevalent, yet medicinally underappreciated, cyanobacterial protease inhibitor scaffold and undertook comprehensive protease profiling to reveal potent and selective elastase inhibition. Structure-activity relationship (SAR) studies and X-ray cocrystal structure analysis allowed a detailed assessment
Brian P O'Sullivan et al.
The Journal of pediatrics, 162(4), 808-812 (2012-12-19)
To describe pancreatic function during the first year of life in infants diagnosed with cystic fibrosis (CF) using serial fecal elastase measurements. This was a longitudinal study of 82 infants diagnosed with CF through newborn screening. Monthly stool samples were

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