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Merck

E0258

Elastase from porcine pancreas

Type IV, Protein 50-90 %, lyophilized powder, ≥4.0 units/mg protein (biuret)

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:
Specific activity:
≥4.0 units/mg protein (biuret)
Biological source:
Porcine pancreas
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biological source

Porcine pancreas

Quality Segment

type

Type IV

form

lyophilized powder

specific activity

≥4.0 units/mg protein (biuret)

composition

Protein, 50-90%

foreign activity

trypsin ≤50 BAEE units/mg protein

storage temp.

−20°C

General description

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.

Application

Elastase from porcine pancreas has been used:
  • to treat vero cells to study its effects on syncytium formation
  • as a positive control in protease assays
  • as a component in RPMI 1640 to isolate human aortic smooth muscle cells (HASMCs) from the aortic tissue

Elastase from Sigma has been used to examine the extent of proteolytic degradation of BSA that is treated with hydroxyl radical. It has also been used to purify elastase-inhibitory lipid derivative from a cyanobacterium, Microcystis Ku2.
Elastase from porcine pancreas has been used in a study to assess the molecular bases for human leucocyte elastase inhibition. Elastase from porcine pancreas has also been used in a study to investigate the molecular cloning and expression of serum calcium-decreasing factor (caldecrin).

Biochem/physiol Actions

Elastase is a serine protease with broad specificity as 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. Elastase hydrolyses elastin, the specific protein of elastic fibers, and digests hemoglobin, casein and fibrin.
Elastase hydrolyses elastin, the specific protein of elastic fibers, and digests hemoglobin, casein and fibrin.
Elastase is a serine protease with broad specificity as 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

Physical form

Contains sodium carbonate.

Preparation Note

A further purification of Type III, E 0127, by affinity chromatography to reduce trypsin activity

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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pictograms

Health hazardExclamation mark

signalword

Danger

Hazard Classifications

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

target_organs

Respiratory system

Klasa składowania

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable



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