Skip to Content
Merck
All Photos(1)

Documents

P6911

Sigma-Aldrich

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


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

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.

Pictograms

Health hazardExclamation mark

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.

Visit the Document Library

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
P Bressollier et al.
Applied and environmental microbiology, 65(6), 2570-2576 (1999-05-29)
Streptomyces strain K1-02, which was identified as a strain of Streptomyces albidoflavus, secreted at least six extracellular proteases when it was cultured on feather meal-based medium. The major keratinolytic serine proteinase was purified to homogeneity by a two-step procedure. This
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
Jian-Hua Wang et al.
Journal of virology, 81(17), 8933-8943 (2007-06-15)
Dendritic cells (DCs) potently stimulate the transmission of human immunodeficiency virus type 1 (HIV-1) to CD4(+) T cells. Immature DCs (iDCs) located in submucosal tissues can capture HIV-1 and migrate to lymphoid tissues, where they become mature DCs (mDCs) for

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