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E0258

Sigma-Aldrich

Elastase from porcine pancreas

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

Synonyme(s) :

Elastase from hog pancreas, Pancreatopeptidase E

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Source biologique

Porcine pancreas

Type

Type IV

Forme

lyophilized powder

Activité spécifique

≥4.0 units/mg protein (biuret)

Composition

Protein, 50-90%

Activité étrangère

trypsin ≤50 BAEE units/mg protein

Température de stockage

−20°C

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Description générale

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

Actions biochimiques/physiologiques

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.

Conditionnement

Package size based on protein content

Définition de l'unité

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

Forme physique

Contains sodium carbonate.

Notes préparatoires

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

Pictogrammes

Health hazardExclamation mark

Mention d'avertissement

Danger

Mentions de danger

Classification des risques

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

Organes cibles

Respiratory system

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

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
Elastase Digests: New Ammunition for Shotgun Membrane xn-ProteomicsS-ig5f
Rietschel B, et al.
Molecular and Cellular Proteomics, 8(5), 1029-1029 (2009)
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)
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)

Protocoles

Enzymatic Assay of Elastase (EC 3.4.21.36), a continuous spectrophotometric rate determination.

Enzymatic Assay of Elastase (EC 3.4.21.36), a continuous spectrophotometric rate determination.

Enzymatic Assay of Elastase (EC 3.4.21.36), a continuous spectrophotometric rate determination.

Enzymatic Assay of Elastase (EC 3.4.21.36), a continuous spectrophotometric rate determination.

Chromatograms

application for HPLC

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