T7902
Thermolysin from Geobacillus stearothermophilus
powder, BioReagent, 30-350 units/mg protein (E1%/280), suitable for cell culture
Synonym(s):
Protease from Geobacillus stearothermophilus, Thermophilic-bacterial protease
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About This Item
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biological source
Geobacillus stearothermophilus
Quality Level
product line
BioReagent
form
powder
specific activity
30-350 units/mg protein (E1%/280)
mol wt
34.6 kDa
purified by
crystallization
technique(s)
cell culture | mammalian: suitable
single cell analysis: suitable
storage temp.
−20°C
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Application
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.
Unit Definition
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).
Physical form
lyophilized powder containing calcium and sodium acetate buffer salts
inhibitor
Product No.
Description
Pricing
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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Journal of biochemistry, 152(3), 231-239 (2012-06-01)
In the N-terminal domain of thermolysin, two anti-parallel β-strands, Asn112-Ala113-Phe114-Trp115 and Ser118-Gln119-Met120-Val121-Tyr122 are connected by an Asn116-Gly117 turn to form a β-hairpin structure. In this study, we examined the role of Asn116 in the activity and stability of thermolysin by
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Acta crystallographica. Section D, Biological crystallography, 68(Pt 11), 1584-1587 (2012-10-24)
An electrospun liquid microjet has been developed that delivers protein microcrystal suspensions at flow rates of 0.14-3.1 µl min(-1) to perform serial femtosecond crystallography (SFX) studies with X-ray lasers. Thermolysin microcrystals flowed at 0.17 µl min(-1) and diffracted to beyond
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