E0258
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
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About This Item
CAS Number:
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
Product Name
Elastase from porcine pancreas, Type IV, Protein 50-90 %, lyophilized powder, ≥4.0 units/mg protein (biuret)
biological source
Porcine pancreas
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
Quality Level
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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
Biochem/physiol Actions
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.
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.
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.
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.
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
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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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)
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)
N Rugani et al.
Biochimica et biophysica acta, 1247(2), 185-194 (1995-03-15)
Porcine colipase, the protein cofactor of pancreatic lipase, was isolated from pancreas freshly collected on animals and from a side fraction from the production of insulin (Novo Nordisk A/S). Samples of purified colipase were analyzed for homogeneity by polyacrylamide gel
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