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Elastase from porcine pancreas

SIGMA/E1250 - Type I, ≥4.0 units/mg protein

Synonym: Elastase from hog pancreas; Pancreatopeptidase E

CAS Number: 39445-21-1
EC Number: 254-453-6
MDL Number: MFCD00130998
Product Type: Chemical

Catalog Number PKG Qty. Price Quantity
45-E1250-10MG 10 mg
$69.50
1/EA
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45-E1250-25MG 25 mg
$115.00
1/EA
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45-E1250-50MG 50 mg
$204.00
1/EA
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45-E1250-100MG 100 mg
$354.00
1/EA
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45-E1250-500MG 500 mg
$1490.00
1/EA
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This image is provided for informative purposes only and does not represent an actual product label. It should not be used as a substitute for official product labeling.

 

biological source Porcine pancreas
concentration 0.5-15.0 mg/mL in water
contains 0.1% thymol
foreign activity trypsin ≤50 BAEE units/mg protein
form suspension
mol wt 25.9 kDa
Quality Level 200 
specific activity ≥4.0 units/mg protein
storage temp. 2-8°C
type Type I
Application: Elastase from porcine pancreas has been used in a study to investigate the design, synthesis and evaluation of biomimetic affinity ligands for elastases. Elastase from porcine pancreas has also been used in a study to investigate the purification and partial characterization of the pancreatic proteolytic enzymes trypsin, chymotrypsin, and elastase.
Application: Elastase from porcine pancreas has been used:
• to induce abdominal aortic aneurysm (AAA)
• to study the impact of indoleamine 2-3 dioxygenase 1 (IDO) in mice
• to digest aortas for aortic smooth muscle cells (SMC) isolation
• as a positive control of proteolytic digestion

Application: The enzyme from Sigma has been used in the development of elastase-perfused animal model . This study determined if tobacco exposure could lower the threshold of aortic injury necessary for AAA (abdominal aortic aneurysm) development. It has also been used during the isolation of type II pneumocytes from human lungs.
Biochem/physiol Actions: Elastase hydrolyses elastin, the specific protein of elastic fibers, and digests hemoglobin, casein and fibrin.
Biochem/physiol Actions: Elastase is a single polypeptide chain of 240 amino acid residues and contains four disulfide bridges. The molecular mass is approximately 25.9 kDa. The enzyme is synthesized as an inactive zymogen, proelastase, which is converted to the active form by limited proteolysis at the N-terminal by trypsin. It is a serine protease with broad specificity. It cleaves protein at the carboxyl side of small hydrophobic amino acids such as Ile, Gly, Ala, Ser, Val, and Leu. The enzyme also hydrolyzes amides and esters such as N-Benzoyl-L-alanine methyl ester. The pH optimum is found to be 8.0-8.5. It does not require any activator, but it is inhibited by diisopropyl fluorophosphate, phenylmethanesulfonyl fluoride, α2-macroglobulin, α1-antitrypsin, sulfonyl fluorides and p-dinitrophenyl diethylphosphate and high salt concentrations. It is extensively used in tissue and cell dissociation procedures. Elastase is effective in the isolation of Type II lung cells.
Other Notes: One unit will hydrolyze 1.0 μmole of N-succinyl-L-Ala-Ala-Ala-p-nitroanilide per min, pH 8.0 at 25 °C.
Packaging: Package size based on protein content
Preparation Note: 2× crystallized
activity specific activity: ≥4.0 units/mg protein
Storage Temp. 2-8°C
Enzyme Commission (EC) Number 3.4.21.36   ( BRENDA  | IUBMB  )
UNSPSC 12352204

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