MilliporeSigma
All Photos(3)

Documents

E0258

Sigma-Aldrich

Elastase from porcine pancreas

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

Sign Into View Organizational & Contract Pricing

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

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

Looking for similar products? Visit Product Comparison Guide

Related Categories

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

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.

Packaging

Package size based on protein content

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

signalword

Danger

Hazard Classifications

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

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Documents related to the products that you have purchased in the past have been gathered in the Document Library for your convenience.

Visit the Document Library

Difficulty Finding Your Product Or Lot/Batch Number?

Product numbers are combined with Pack Sizes/Quantity when displayed on the website (example: T1503-25G). Please make sure you enter ONLY the product number in the Product Number field (example: T1503).

Example:

T1503
Product Number
-
25G
Pack Size/Quantity

Additional examples:

705578-5MG-PW

PL860-CGA/SHF-1EA

MMYOMAG-74K-13

1000309185

enter as 1.000309185)

Having trouble? Feel free to contact Technical Service for assistance.

Lot and Batch Numbers can be found on a product's label following the words 'Lot' or 'Batch'.

Aldrich Products

  • For a lot number such as TO09019TO, enter it as 09019TO (without the first two letters 'TO').

  • For a lot number with a filling-code such as 05427ES-021, enter it as 05427ES (without the filling-code '-021').

  • For a lot number with a filling-code such as STBB0728K9, enter it as STBB0728 without the filling-code 'K9'.

Not Finding What You Are Looking For?

In some cases, a COA may not be available online. If your search was unable to find the COA you can request one.

Request COA

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service