E0258

Sigma-Aldrich

Elastase from porcine pancreas

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

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

Quality Level

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

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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 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).
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

Packaging

1, 5, 10, 20, 50 mg in glass bottle
Package size based on protein content

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 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.

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

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

Pictograms

Exclamation markHealth hazard

Signal Word

Danger

Hazard Statements

Target Organs

Respiratory system

RIDADR

NONH for all modes of transport

WGK Germany

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis

Certificate of Origin

Pancreatic elastases
Handbook of Proteolytic Enzymes, 2639-2645 (2013)
Evidence for the amino acid sequence of porcine pancreatic elastase
Shotton DM and Hartley BS
The Biochemical Journal, 131(4), 643-643 (1973)
Suvendra Nath Bagchi et al.
Indian journal of microbiology, 51(4), 496-500 (2012-10-02)
A unicyanobacterial isolate of cyanobacterium, identified as Microcystis Ku2, produced a mammalian elastase-inhibitory lipid derivative. Protease inhibitors in cyanobacteria are unequivocally peptides. Since this metabolite appeared in lipid phase, we worked on a hypothesis that whether metabolite other than peptides...
Digestive enzymes and stylet morphology of Deraeocoris nebulosus (Hemiptera: Miridae), a predacious plant bug
Boyd DW, et al.
Annals of the Entomological Society of America, 395-401 (2002)
Elastase Digests: New Ammunition for Shotgun Membrane xn-ProteomicsS-ig5f
Rietschel B, et al.
Molecular and Cellular Proteomics, 8(5), 1029-1029 (2009)
Protocols
Enzymatic Assay of Elastase (EC 3.4.21.36), a continuous spectrophotometric rate determination.
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