Protease from Bacillus licheniformis, >=2.4 U/g

Code: p4860-250ml D2-231

Not available outside of the UK & Ireland.

Analysis Note

Activity expressed in Anson Units

Application

Protease is an enzyme used to break down proteins by hydrolyzing peptide bonds. Prote...


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Your Price
$263.90 250ML

Not available outside of the UK & Ireland.

Analysis Note

Activity expressed in Anson Units

Application

Protease is an enzyme used to break down proteins by hydrolyzing peptide bonds. Protease is used to degrade proteins, to study protease inhibitors and to study thermal inactivation kinetics. Protease is used in nucleic acid isolation procedures in incubations.

The enzyme from Sigma has been used to prepare chicken (leg) bone protein hydrolysates while evaluating ACE inhibitory peptides. It has also been used for the hydrolysis of Chlorella pyrenoidosa protein extracts during a study of their antitumor activities.

Biochem/physiol Actions

Protease catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate .

Alcalase is an endo-protease of the serine type. It has a broad substrate specificity and can hydrolyze most peptide bonds within a protein molecule. It is active between pH 6.5 and 8.5 and has an optimum temperature of 60 °C. The enzyme is is used in detergent formulations to remove protein-based stains.

General description

Proteolytic enzymes are known to possess catalytic, non-catalytic and ancillary domains. Proteases are broadly classified as endopeptidases and exopeptidases. Functionally they are divided as aspartic, glutamic, cysteine, threonine, serine and metalloproteases.

Legal Information

A product of Novozyme Corp.

Alcalase is a registered trademark of Novozymes Corp.

formaqueous solution
Quality Level200
specific activity≥2.4 U/g
storage temp.2-8°C
Code
Description
Unit Size
List Price
Qty
P4860-50ML
Unit:50ML
List Price: $110.35
Source:List Price
ADD
Cas Number9014-01-1
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