P6911

Protease from Streptomyces griseus

BioReagent, DNase, RNase, and nickase, none detected (No RNase.)

• Synonym(s): Actinase E, Pronase E
• CAS Number: 9036-06-0
• UNSPSC Code: 12352204
• eCl@ss: 32160410
• EC Number: 232-909-5
• NACRES: NA.21
• MDL number: MFCD00132092
• Concentration: ≥4 unit/mg

Properties

• grade: Molecular Biology
• Quality Level: 200
• product line: BioReagent
• form: powder
• mol wt: monomer ~20 kDa
• concentration: ≥4 unit/mg
• solubility: water: 5-20 mg/mL
• foreign activity: DNase, RNase, and nickase, none detected (No RNase.)
• storage temp.: −20°C

Description

General description

A mixture of at least three proteolytic activities including an extracellular serine protease. In general, serine proteases display a wide range of substrate specificities, which are believed to be mediated by an active site composed of one Asp, one His, and a Ser residue in the molecule. This enzyme prefers to hydrolyze peptide bonds on the carboxyl side of glutamic or aspartic acid.

Completely inactivated by heating above 80 °C for 15-20 minutes.

Application

Protease is typically used in nucleic acid isolation procedures in incubations of 0.5-3.0 hours supplemented with 0.2% sodium dodecyl sulfate and 10 mM EDTA.

Suitable for:

• Nucleic acid isolation procedures in incubations
• Degrade protein during nucleic acid purification
• Proteolysis of insoluble protein
• Structural protein studies

This enzyme is more active at a higher pH range than the known alkaline protease, showing the proteolytic activity even in 0.2N NaOH solution. This enzyme is useful for proteolysis of insoluble protein and for structure investigation of protein.

Biochem/physiol Actions

A mixture of at least three proteolytic activities including an extracellular serine protease. In general, serine proteases display a wide range of substrate specificities, which are believed to be mediated by an active site composed of one Asp, one His, and a Ser residue in the molecule. This enzyme prefers to hydrolyze peptide bonds on the carboxyl side of glutamic or aspartic acid.

Preparation Note

Collected from culture broth of S. griseus.

Analysis Note

The protease is incubated for 10 minutes at pH 7.5 at 37°C in a 6 ml reaction volume containing 0.54% casein and 0.041 M potassium phosphate buffer. The reaction is stopped by the addition of 5.0 ml of 0.11 M trichloroacetic acid.

Other Notes

One unit will hydrolyze casein to produce color equivalent to 1.0 μmole (181 μg) of tyrosine per min at pH 7.5 at 37 °C (color by Folin-Ciocalteu reagent).

This protease is completely inactivated by heating above 80°C for 15-20 minutes. This enzyme is more active at a higher pH range, showing the proteolytic activity even in 0.2N NaOH solution.

Safety Information

• pictograms: GHS08,GHS07
• signalword: Danger
• hcodes: H315,H319,H334,H335
• pcodes: P302 + P352 - P305 + P351 + P338
• 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 2
• flash_point_f: Not applicable
• flash_point_c: Not applicable
• ppe: Eyeshields, Gloves, type N95 (US)