P6911
Protease from Streptomyces griseus
BioReagent, DNase, RNase, and nickase, none detected (No RNase.)
Synonym(s):
Actinase E, Pronase E
Sign Into View Organizational & Contract Pricing
All Photos(1)
About This Item
CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.21
Recommended Products
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
Looking for similar products? Visit Product Comparison Guide
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
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Customers Also Viewed
Hyun-Ju Cho et al.
Disease models & mechanisms, 12(5) (2019-05-03)
DYRK1A is a major causative gene in Down syndrome (DS). Reduced incidence of solid tumors such as neuroblastoma in DS patients and increased vascular anomalies in DS fetuses suggest a potential role of DYRK1A in angiogenic processes, but in vivo
Laura Rennert et al.
Frontiers in immunology, 9, 1589-1589 (2018-08-01)
Endogenously released adenosine-5'-triphosphate (ATP) is a key regulator of physiological function and inflammatory responses in the kidney. Genetic or pharmacological inhibition of purinergic receptors has been linked to attenuation of inflammatory disorders and hence constitutes promising new avenues for halting
Livio Dukaj et al.
PLoS genetics, 17(3), e1009467-e1009467 (2021-03-26)
Loading of the MCM replicative helicase at origins of replication is a highly regulated process that precedes DNA replication in all eukaryotes. The stoichiometry of MCM loaded at origins has been proposed to be a key determinant of when those
D Colombatto et al.
Journal of animal science, 81(10), 2617-2627 (2003-10-14)
A dual-flow continuous culture system was used to investigate the effects of pH and addition of an enzyme mixture to a total mixed ration (TMR) on fermentation, nutrient digestion, and microbial protein synthesis. A 4 x 4 Latin square design
O Almog et al.
Journal of molecular biology, 230(1), 342-344 (1993-03-05)
Streptomyces griseus excretes a small molecular mass (30 kDa) aminopeptidase that could be used for various biotechnological applications. This enzyme was isolated from an extracellular protease mixture of Streptomyces griseus (Pronase E. Sigma) and single crystals were obtained by the
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service