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P1512

Thermolysin from Geobacillus stearothermophilus

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

Synonyme(s) :

Protease from Geobacillus stearothermophilus, Thermophilic-bacterial protease

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A propos de cet article

Numéro CAS:
UNSPSC Code:
12352204
eCl@ss:
32160410
EC Number:
232-973-4
NACRES:
NA.54
MDL number:
Numéro CE :
Specific activity:
30-350 units/mg protein (E1%/280)
Biological source:
Geobacillus stearothermophilus
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biological source

Geobacillus stearothermophilus

Quality Segment

type

Type X

form

lyophilized powder

specific activity

30-350 units/mg protein (E1%/280)

mol wt

34.6 kDa by amino acid sequence

purified by

crystallization

shipped in

wet ice

storage temp.

−20°C

General description

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

Application

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.
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.

Physical form

lyophilized powder containing calcium and sodium acetate buffer salts

Preparation Note

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.

Analysis Note

Contains many extraneous enzymes.

Other Notes

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).


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Mot-clé

Danger

Classe de stockage

11 - Combustible Solids

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

EPI (équipement de protection individuelle)

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

Organes cibles

Respiratory system

Pictogrammes

Health hazardExclamation mark

Codes de danger

Hazard Classifications

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

Que se passe-t-il ?

WGK 1



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