Skip to Content
Merck
All Photos(1)

Documents

45125

Sigma-Aldrich

Elastase from porcine pancreas

lyophilized, powder, white, ~8 U/mg

Synonym(s):

Elastase from hog pancreas, Pancreatopeptidase E

Sign Into View Organizational & Contract Pricing


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

Looking for similar products? Visit Product Comparison Guide

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
Sales restrictions may apply

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’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

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)
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
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
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

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service