P1512
Thermolysin from Geobacillus stearothermophilus
Type X, lyophilized powder, 30-350 units/mg protein (E1%/280)
Sinonimo/i:
Protease from Geobacillus stearothermophilus, Thermophilic-bacterial protease
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About This Item
Prodotti consigliati
Origine biologica
Geobacillus stearothermophilus
Livello qualitativo
Tipo
Type X
Stato
lyophilized powder
Attività specifica
30-350 units/mg protein (E1%/280)
PM
34.6 kDa by amino acid sequence
Purificato mediante
crystallization
Condizioni di spedizione
wet ice
Temperatura di conservazione
−20°C
Categorie correlate
Descrizione generale
Thermolysin is a protease that has specificity different from other proteases available for sequence investigations.
Applicazioni
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.
Qualità
Contains many extraneous enzymes.
Definizione di unità
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).
Stato fisico
lyophilized powder containing calcium and sodium acetate buffer salts
Nota sulla preparazione
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.
Avvertenze
Danger
Indicazioni di pericolo
Consigli di prudenza
Classi di pericolo
Resp. Sens. 1
Codice della classe di stoccaggio
11 - Combustible Solids
Classe di pericolosità dell'acqua (WGK)
WGK 3
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
Dispositivi di protezione individuale
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
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I clienti hanno visto anche
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
The use of thermolysin in amino acid sequence determination.
R P Ambler et al.
The Biochemical journal, 108(5), 893-895 (1968-08-01)
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
Balbir K Chaal et al.
Methods in molecular biology (Clifton, N.J.), 390, 207-217 (2007-10-24)
All the algae with chlorophyll (Chl) c (haptophytes, cryptophytes, and heterokonts such as diatoms) acquired their chloroplasts by secondary endosymbiosis, where a nonphotosynthetic eukaryote host engulfed (or was invaded by) a red alga. This resulted in chloroplasts with four bounding
Haley Marshall et al.
Acta crystallographica. Section D, Biological crystallography, 68(Pt 1), 69-81 (2011-12-24)
Both crystallization and cryoprotection are often bottlenecks for high-resolution X-ray structure determination of macromolecules. Methylamine osmolytes are known stabilizers of protein structure. One such osmolyte, trimethylamine N-oxide (TMAO), has seen occasional use as an additive to improve macromolecular crystal quality
Protocolli
To standardize a procedure for the enzymatic assay of Protease using Casein as a substrate.
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