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Merck

P1512

Sigma-Aldrich

Thermolysin from Geobacillus stearothermophilus

Type X, lyophilized powder, 30-350 units/mg protein (E1%/280)

Synonim(y):

Protease from Geobacillus stearothermophilus, Thermophilic-bacterial protease

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About This Item

Numer CAS:
Numer EC enzymu:
Numer WE:
Numer MDL:
Kod UNSPSC:
12352204
eCl@ss:
32160410
NACRES:
NA.54

pochodzenie biologiczne

Geobacillus stearothermophilus

typ

Type X

Postać

lyophilized powder

aktywność właściwa

30-350 units/mg protein (E1%/280)

masa cząsteczkowa

34.6 kDa by amino acid sequence

oczyszczone przez

crystallization

Warunki transportu

wet ice

temp. przechowywania

−20°C

Opis ogólny

Thermolysin is a protease that has specificity different from other proteases available for sequence investigations.

Zastosowanie

A thermostable (thermophilic) extracellular metalloendopeptidase containing four calcium ions. Cofactors are zinc and calcium. Hydrolyzes protein bonds on the N-terminal side of hydrophobic amino acid residues. The pH optimum is 8.0 and the optimal temperature for activity is 70 °C. Considerably stable from pH 5 to 9.5. Thermolysin has a low cleavage specificity, therefore, it produces a number of short fragments that are suitable for sequencing. Preferential cleavage: X-cleavage-Y-Z where X=any amino acid; Y=Leu, Phe, Ile, Val, Met, Ala and Z is any amino acid other than Pro. Cleavage N-terminal to Leu is preferred over cleavage of N-terminal to Phe which is preferred over the others. Often used to do limited proteolysis for peptide mapping and studies of protein structure and conformational changes.
Thermolysin has been shown to have a prosequeence that acts as an intramolecular chaperone in vivo. It has also been used in a study to investigate the effects of sodium chloride on thermal stability and catalytic activity.
Thermolysin is also commonly used for the commercial synthesis of N-(benzyloxycarbonyl)-L-aspartyl-L-phenylalanine methyl ester, the precursor for the artificial sweetener aspartame.

Jakość

Contains many extraneous enzymes.

Definicja jednostki

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).

Postać fizyczna

lyophilized powder containing calcium and sodium acetate buffer salts

Uwaga dotycząca przygotowania

The pH optimum is 8.0 and the optimal temperature for activity is 70 °C. Considerably stable from pH 5 to 9.5. Thermolysin has a low cleavage specificity, therefore, it produces a number of short fragments that are suitable for sequencing. Preferential cleavage: X-cleavage-Y-Z where X=any amino acid; Y=Leu, Phe, Ile, Val, Met, Ala and Z is any amino acid other than Pro. Cleavage N-terminal to Leu is preferred over cleavage of N-terminal to Phe which is preferred over the others.
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Piktogramy

Health hazard

Hasło ostrzegawcze

Danger

Zwroty wskazujące rodzaj zagrożenia

Zwroty wskazujące środki ostrożności

Klasyfikacja zagrożeń

Resp. Sens. 1

Kod klasy składowania

11 - Combustible Solids

Klasa zagrożenia wodnego (WGK)

WGK 3

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable

Środki ochrony indywidualnej

dust mask type N95 (US), Eyeshields, Faceshields, Gloves


Certyfikaty analizy (CoA)

Poszukaj Certyfikaty analizy (CoA), wpisując numer partii/serii produktów. Numery serii i partii można znaleźć na etykiecie produktu po słowach „seria” lub „partia”.

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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

Maria Fernanda Lay Mendoza et al.
Viruses, 12(12) (2020-12-23)
Viral entry is the first stage in the virus replication cycle and, for enveloped viruses, is mediated by virally encoded glycoproteins. Viral glycoproteins have different receptor affinities and triggering mechanisms. We employed vesicular stomatitis virus (VSV), a BSL-2 enveloped virus
C Marie-Claire et al.
Journal of molecular biology, 285(5), 1911-1915 (1999-02-02)
The zinc metalloendopeptidase, thermolysin (EC 3.4.24.27) produced by Bacillus thermoproteolyticus serves as a model of important physiological enzymes such as neprilysin, angiotensin converting enzyme and endothelin converting enzyme. Thermolysin is synthesised as a pre-proenzyme, with an N-terminal prosequence of 204
Chiwook Park et al.
Nature methods, 2(3), 207-212 (2005-03-23)
Thermodynamic stability is fundamental to the biology of proteins. Information on protein stability is essential for studying protein structure and folding and can also be used indirectly to monitor protein-ligand or protein-protein interactions. While clearly valuable, the experimental determination of
M Miyanaga et al.
Biotechnology and bioengineering, 46(6), 631-635 (1995-06-20)
N-(benzyloxycarbonyl)-L-aspartyl-L-phenylalanine methyl ester, a precursor of the synthetic sweetener, aspartame, was synthesized from N-(benzyloxycarbonyl)-L-aspartic acid and L-phenylalanine methyl ester with an immobilized thermolysin (EC 3.4.24.4) in the mixed organic solvent system of tert-amyl alcohol and ethyl acetate. A mixed solvent
Yongjin Park et al.
Scientific reports, 12(1), 10935-10935 (2022-06-30)
Long wavelengths that can deeply penetrate into human skin are required to maximize therapeutic effects. Hence, various studies on near-infrared organic light-emitting diodes (NIR OLEDs) have been conducted, and they have been applied in numerous fields. This paper presents a

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