P6911
Protease from Streptomyces griseus
BioReagent, DNase, RNase, and nickase, none detected (No RNase.)
Synonym(s):
Actinase E, Pronase E
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About This Item
CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.21
grade
for molecular biology
Quality Level
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
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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.
Specificity
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.
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.
Physical properties
Completely inactivated by heating above 80 °C for 15-20 minutes.
Unit Definition
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).
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
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.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Target Organs
Respiratory system
Storage Class Code
11 - Combustible Solids
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Listings
Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.
JAN Code
P6911-VAR:
P6911-5G:
P6911-100MG:
P6911-1G-C:
P6911-1G:
P6911-BULK:
Certificates of Analysis (COA)
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D Y Yum et al.
Bioscience, biotechnology, and biochemistry, 58(3), 470-474 (1994-03-01)
SAP, an extracellular alkaline serine protease produced by Streptomyces sp. YSA-130, was purified to homogeneity by CM-Sephadex column chromatography and crystallization. The enzyme was a monomeric protein with a molecular weight of 19,000 as estimated by SDS-PAGE and gel filtration.
N Yoshida et al.
Journal of biochemistry, 104(3), 451-456 (1988-09-01)
A protease was purified 163-fold from Pronase, a commercial product from culture filtrate of Streptomyces griseus, by a series of column chromatographies on CM-Toyopearl (Fractogel), Sephadex G-50, hydroxyapatite, and Z-Gly-D-Phe-AH-Sepharose 4B using Boc-Ala-Ala-Pro-Glu-pNA as a substrate. The final preparation was
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