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P0652

Sigma-Aldrich

Protease from Streptomyces sp.

Type XXI, ≥15 units/mg solid

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Synonym(s):
actinase E, pronase E, Actinase E, Pronase E
CAS Number:
EC Number:
MDL number:
NACRES:
NA.54

type

Type XXI

Quality Level

form

powder

specific activity

≥15 units/mg solid

mol wt

~50 kDa

storage temp.

−20°C

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This Item
P5147P8811537088
Protease from Streptomyces sp. Type XXI, ≥15 units/mg solid

P0652

Protease from Streptomyces sp.

Protease from Streptomyces griseus Type XIV, ≥3.5 units/mg solid, powder

P5147

Protease from Streptomyces griseus

Protease from Streptomyces griseus powder, BioReagent, suitable for mouse embryo cell culture, ≥3.5 units/mg solid

P8811

Protease from Streptomyces griseus

form

powder

form

powder

form

powder

form

lyophilized

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

2-8°C

mol wt

~50 kDa

mol wt

-

mol wt

-

mol wt

-

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

-

type

Type XXI

type

Type XIV

type

-

type

-

Application

Pronase E can be used to degrade antheraea pernyi silk fibroin films.
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.
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.
This enzyme is useful for proteolysis of insoluble protein and for structure investigation of protein. Proteases from Streptomyces griseus and Streptomyces omiyaensis have been used in a study to identify residue 71 as a crucial residue for differences in topological specificities. Proteases have also been used in a study to investigate production of protease as a by-product of streptomycin production.

Biochem/physiol Actions

Alkaline protease that is approximately twice as active at pH 11.0 than at the usual assay conditions for protease, pH 7.5 and 37 °C. By comparison, P5147 Type XIV protease is only approximately 25% as active at pH 11.0, 30 °C.

Physical properties

Isoelectric point : 8.7
Inhibitors : Diisopropyl fluorophosphate, EDTA
Optimum pH : >=12
Optimum temperature : 60oC
pH Stability : pH 5.0 - 11.5 (25oC,24hr)
Thermal stability : below 50oC (pH 8.3, 15min)

Unit Definition

One unit will hydrolyze casein to produce peptide equivalent to 1.0 μmole (181 μg) of tyrosine per min at pH 11.0 at 30 °C.

Physical form

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.

Preparation Note

Collected from culture broth of S.Sp

pictograms

Exclamation markHealth hazard

signalword

Danger

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Yoshiko Uesugi et al.
Biochimica et biophysica acta, 1814(10), 1295-1304 (2011-07-20)
We recently identified residue 71 of two homologous serine proteases from Streptomyces omiyaensis (SOT) and Streptomyces griseus (SGT) as a crucial residue for differences in their topological specificities, i.e. recognition of a distinct three-dimensional structure. To study the role of
Paola Taddei et al.
Biomacromolecules, 7(1), 259-267 (2006-01-10)
In this study, Antheraea pernyi silk fibroin (Ap-SF) films were incubated with Protease Type XXI from Streptomyces griseus, at 37 degrees C, to investigate the degradation behavior in an in vitro model system. The enzyme-resistant fractions of Ap-SF films and
A Proteolytic Enzyme of Streptomyces griseus: I. Purification of a Protease of Streptomyces griseus
Nomoto, M. and Y. Narahashi
Biochemistry, 46, 653-667 (1959)
The utility of nonspecific proteases in the characterization of glycoproteins by high-resolution time-of-flight mass spectrometry.
Juhasz, P. and Martin, S.A.
International Journal of Mass Spectrometry and Ion Processes, 169-170, 217-230 (1997)
W W Epstein et al.
Proceedings of the National Academy of Sciences of the United States of America, 87(19), 7352-7354 (1990-10-01)
Prenylated proteins, labeled in the isoprenoid residue by growing CHO cells in medium containing [5-3H]mevalonate, were degraded by three different proteolytic procedures, enzymatic or alkaline hydrolysis as well as hydrazinolysis. The products thus obtained were analyzed by HPLC with chemically

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