PROTEASE Chemical Properties

storage temp. 

2-8°C

solubility 

H₂O: 5-20 mg/mL

form 

powder

color 

white

biological source

Bacillus sp. (Bacillus amyloliquefaciens)

Specific Activity

≥0.8U/g

Safety Information

Hazard Codes 

Xn

Risk Statements 

37/38-41-42-36/37/38-42/43-20-50-22

Safety Statements 

23-24-26-36/37/39-36/37-22-36-45-61

WGK Germany 

3

RTECS 

UK9595000

F 

3-10

MSDS

• Language:English Provider:SigmaAldrich

PROTEASE Usage And Synthesis

Uses

Protease from Bacillus amyloliquefaciens has been used for the unhairing of hides and skins. It has also been used in a study to investigate peptide bond formation using the carbamoylmethyl ester as the acyl donor.

General Description

Bacterial protease produced by submerged fermentation of a selected strain of Bacillus amyloliquefaciens

Biochem/physiol Actions

Secretion of protease by Bacillus amyloliquefaciens can be inhibited by treatment with the fatty acid synthetase inhibitor cerulenin.

Toxics Screening Level

The initial threshold screening level (ITSL) for subtilisins is 0.0006 μg/m 3 (1-hour averaging time).

Description

Protease Recombinant is a fusion protein of glutathione S-transferase (GST) and human rhinovirus (HRV) type 14 3C protease. The protease specifically recognizes a subset of sequences which include the core amino acid sequence Leu-Phe-Gln/Gly-Pro cleaving between the Gln and Gly residues. Substrate recognition and cleavage are likely to be dependent not only upon primary structural signals, but also upon the secondary and tertiary structures of the fusion protein as well.
The Recombinant Protease is purified by proprietary chromatographic techniques.

Source

Escherichia Coli

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