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E0258

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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A propos de cet article

Numéro CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
254-453-6
MDL number:
Numéro CE :
Specific activity:
≥4.0 units/mg protein (biuret)
Biological source:
Porcine pancreas
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biological source

Porcine pancreas

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

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[1]
  • 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.[2] It has also been used to purify elastase-inhibitory lipid derivative from a cyanobacterium, Microcystis Ku2.[3]
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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Cet article
E7885E0127E1250
specific activity

≥4.0 units/mg protein (biuret)

specific activity

≥4 units/mg protein

specific activity

≥4.0 units/mg protein

specific activity

≥4.0 units/mg protein

biological source

Porcine pancreas

biological source

Porcine

biological source

-

biological source

Porcine pancreas

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

suspension

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

2-8°C

foreign activity

trypsin ≤50 BAEE units/mg protein

foreign activity

Trypsin ≤50 BAEE units/mg protein

foreign activity

-

foreign activity

trypsin ≤50 BAEE units/mg protein

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200


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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

Classe de stockage

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable



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Consulter la Bibliothèque de documents



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)
Cloning and overexpression of extracellular elastase from Pseudomonas aeruginosa
Raftari M, et al.
European journal of inflammation, 11(1), 55-60 (2013)



Numéro d'article de commerce international

RéférenceGTIN
E0258-5MG04061833601013
E0258-1MG04061826674598
E0258-20MG04061833601006
E0258-10MG04061833600993
E0258-50MG04061832700571

Questions

  1. How does this product (elastase type IV) needs to be dissolved?

    1 answer
    1. This product can be resuspended in pH 8 Tris buffer, as mentioned on the Enzymatic Assay of Elastase webpage. For more details, please refer to the following link: https://www.sigmaaldrich.com/technical-documents/protocol/protein-biology/enzyme-activity-assays/enzymatic-assay-of-elastase#preparation

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