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324682
Sigma-AldrichElastase, Porcine Pancreas, High Purity, Crystallized
Elastase, Porcine Pancreas, High Purity, Crystallized, CAS 39445-21-1, is a serine protease that hydrolyzes proteins and peptides, especially at bonds adjacent to neutral amino acid residues.
More>>Elastase, Porcine Pancreas, High Purity, Crystallized, CAS 39445-21-1, is a serine protease that hydrolyzes proteins and peptides, especially at bonds adjacent to neutral amino acid residues. Less<<
MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.
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Description
Overview
Native elastase from porcine pancreas. A serine protase that catalyzes the hydrolysis of proteins and peptides (especially at bonds adjacent to neutral amino acid residues), including albumin, casein, denatured collagen, elastin, fibrin, and hemoglobin and of a number of synthetic substrates containing aspartic acid, phenylalanine, or tyrosine. Inhibited by DFP, elastinal, and α2-macroglobulin.
Catalogue Number
324682
Brand Family
Calbiochem®
References
References
Largman, C. et al. 1976. Biochemestry15, 2491. Mandl, I. 1962. Methods in Enzymol.5, 665.
Product Information
CAS number
39445-21-1
Unit of Definition
One unit is defined as the amount of enzyme that will hydrolyze 1.0 µmol of Suc-Ala-Ala-Pro-Abu-<i>p</i>NA (<a href = "/Products/ProductDisplay.asp→catNO=324699">Cat. No. 324699</a>) per min at 25°C, pH 8.0.
EC number
3.4.21.36
Form
Lyophilized
Formulation
Lyophilized from 50 mM Trehalose, 1 mM Acetic Acid.
Following reconstitution, elastase may be stored at 4°C at pH 6.0 for long term use. If incubated at room temperature at or near its optimum pH, elastase rapidly autolyzes to a mixture of peptides. Stock solutions are stable for up to 2 months at 4°C, pH 6.0.
Packaging Information
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Catalogue Number
GTIN
324682-1000U
04055977196832
324682-250U
07790788054380
Documentation
Elastase, Porcine Pancreas, High Purity, Crystallized SDS
Elastase, Porcine Pancreas, High Purity, Crystallized Certificates of Analysis
Title
Lot Number
324682
References
Reference overview
Largman, C. et al. 1976. Biochemestry15, 2491. Mandl, I. 1962. Methods in Enzymol.5, 665.
Data Sheet
Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.
Revision
09-July-2010 JSW
Description
Native elastase from porcine pancreas. Catalyzes the hydrolysis of proteins and peptides (especially at bonds adjacent to neutral amino acid residues), including albumin, casein, denatured collagen, elastin, fibrin, and hemoglobin, and of a number of synthetic substrates containing aspartic acid, glutamic acid, phenylalanine, or tyrosine. Preferentially cleaves peptide bonds at the carbonyl end of amino acid residues with small hydrophobic side chains, such as glycine, valine, leucine, isoleucine, and particularly alanine. Inhibited by DFP, elastinal, and α2-macroglobulin. Has an optimal pH of 7.8-8.5; pI = 9.5. Note: Elastase tends to adhere to glass. Hence, use of siliconized glassware is recommended.
Form
Lyophilized
Formulation
Lyophilized from 50 mM Trehalose, 1 mM Acetic Acid.
CAS number
39445-21-1
RTECS
TS5052000
EC number
3.4.21.36
Contaminants
Chymotrypsin: ≤0.2%
Specific activity
≥25 units/mg protein
Unit definition
One unit is defined as the amount of enzyme that will hydrolyze 1.0 µmol of Suc-Ala-Ala-Pro-Abu-pNA (Cat. No. 324699) per min at 25°C, pH 8.0.
Solubility
dH₂O (10 mg/ml)
Storage
Protect from moisture -20°C
Do Not Freeze
Ok to freeze
Special Instructions
Following reconstitution, elastase may be stored at 4°C at pH 6.0 for long term use. If incubated at room temperature at or near its optimum pH, elastase rapidly autolyzes to a mixture of peptides. Stock solutions are stable for up to 2 months at 4°C, pH 6.0.
Toxicity
Standard Handling
Merck USA index
14, 3535
References
Largman, C. et al. 1976. Biochemestry15, 2491. Mandl, I. 1962. Methods in Enzymol.5, 665.
