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E0127

Sigma-Aldrich

Elastase from porcine pancreas

Type III, lyophilized powder, Protein 55-85 %, ≥4.0 units/mg protein

Synonym(s):
Elastase from hog pancreas, Pancreatopeptidase E
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
NACRES:
NA.54

type

Type III

Quality Level

form

lyophilized powder

specific activity

≥4.0 units/mg protein

mol wt

25.9 kDa

composition

Protein, 55-85%

solubility

200 mM Tris HCl buffer, pH 8.8: soluble 1.0 mg/mL, clear

storage temp.

−20°C

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This Item
L0382E7885E0258
form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

specific activity

≥4.0 units/mg protein

specific activity

≥20,000 units/mg protein

specific activity

≥4 units/mg protein

specific activity

≥4.0 units/mg protein (biuret)

mol wt

25.9 kDa

mol wt

-

mol wt

25.9 kDa

mol wt

-

solubility

200 mM Tris HCl buffer, pH 8.8: soluble 1.0 mg/mL, clear

solubility

-

solubility

-

solubility

-

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

Quality Level

200

Quality Level

300

Quality Level

200

Quality Level

200

Application

Elastase from porcine pancreas has been used in a study to identify a novel bone/calcium metabolism-regulating factor in porcine pancreas. Elastase from porcine pancreas has also been used in a study to investigate the effect of a specific synthetic inhibitor of neutrophil elastase (ONO-5046) on the course of acute hemorrhagic pancreatitis in dogs.
Elastase from porcine pancreas has been used in the proteolytic cleavage of UMP synthase (Uridine-5′-monophosphate synthase). It has also been used along with collagenase to disperse tissue into single cells from the thoracic media, abdominal aortic media and intima of rabbit.

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, p-dinitrophenyl diethylphosphate and high salt concentrations. Elastase is extensively used in tissue and cell dissociation procedures. It 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.

Packaging

Package size based on protein content

Quality

Contains trypsin activity

Unit Definition

One unit will hydrolyze 1.0 μmole of N-succinyl-L-Ala-Ala-Ala-p-nitroanilide per min, pH 8.0 at 25 °C.

Physical form

Contains sodium carbonate.

Preparation Note

2x crystallized and chromatographically purified

Pictograms

Exclamation markHealth hazard

Signal Word

Danger

Hazard Statements

Hazard Classifications

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

Target Organs

Respiratory system

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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