P1512
Thermolysin from Geobacillus stearothermophilus
Type X, lyophilized powder, 30-350 units/mg protein (E1%/280)
Sinónimos:
Protease from Geobacillus stearothermophilus, Thermophilic-bacterial protease
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About This Item
Productos recomendados
origen biológico
Geobacillus stearothermophilus
Nivel de calidad
tpo
Type X
Formulario
lyophilized powder
actividad específica
30-350 units/mg protein (E1%/280)
mol peso
34.6 kDa by amino acid sequence
purificado por
crystallization
Condiciones de envío
wet ice
temp. de almacenamiento
−20°C
Descripción general
Thermolysin is a protease that has specificity different from other proteases available for sequence investigations.
Aplicación
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.
Calidad
Contains many extraneous enzymes.
Definición de unidad
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).
Forma física
lyophilized powder containing calcium and sodium acetate buffer salts
Nota de preparación
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.
Palabra de señalización
Danger
Frases de peligro
Consejos de prudencia
Clasificaciones de peligro
Resp. Sens. 1
Código de clase de almacenamiento
11 - Combustible Solids
Clase de riesgo para el agua (WGK)
WGK 3
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Equipo de protección personal
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
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Los clientes también vieron
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
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
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
K Inouye et al.
Biochimica et biophysica acta, 1388(1), 209-214 (1998-10-17)
Thermolysin, a thermophilic metalloproteinase, is markedly activated in the presence of high concentrations (1-5 M) of neutral salts. The activity increases in an exponential fashion with increasing salt concentration, and is enhanced 13-15 times with 4 M NaCl at pH
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