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Merck

E1250

Elastase from porcine pancreas

Type I, ≥4.0 units/mg protein

Synonim(y):

Elastase from hog pancreas, Pancreatopeptidase E

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Informacje o tej pozycji

Numer CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
254-453-6
MDL number:
Numer WE:
eCl@ss:
32035490
Specific activity:
≥4.0 units/mg protein
Biological source:
Porcine pancreas
Concentration:
0.5-15.0 mg/mL in water
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biological source

Porcine pancreas

Quality Segment

type

Type I

form

suspension

specific activity

≥4.0 units/mg protein

mol wt

25.9 kDa

contains

0.1% thymol

concentration

0.5-15.0 mg/mL in water

foreign activity

trypsin ≤50 BAEE units/mg protein

storage temp.

2-8°C

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

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.
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.

Biochem/physiol Actions

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

Packaging

Package size based on protein content

Preparation Note

2× crystallized

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.
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Piktogramy

Health hazardExclamation mark

Słowo ostrzegawcze

Danger

Kody zagrożeń

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

Narządy docelowe

Respiratory system

Klasa składowania

11 - Combustible Solids

WGK

WGK 3

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable

PPE (środki ochrony indywidualnej)

dust mask type N95 (US), Eyeshields, Faceshields, Gloves



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