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About This Item
CAS Number:
UNSPSC Code:
12352204
EC Number:
254-453-6
MDL number:
Specific activity:
~8 U/mg
Biological source:
Porcine pancreas
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
Quality Level
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Biochem/physiol Actions
Elastase hydrolyses elastin, the specific protein of elastic fibers, and digests hemoglobin, casein and fibrin.
Other Notes
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)
For protein sequence studies, limited proteolysis; Application in (selective) hydrolysis/condensation of carboxylic ester bonds
One unit will hydrolyze 1.0 μmole of N-succinyl-L-Ala-Ala-Ala-p-nitroanilide per min, pH 8.0 at 25 °C.
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Regulatory Information
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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)
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
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
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