T3330
Thermitase from Bacillus cereus
recombinant, expressed in Bacillus subtilis, enzyme ≥5.0 units/mg protein
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About This Item
UNSPSC Code:
12352204
recombinant
expressed in Bacillus subtilis
form
solid
enzyme activity
≥5.0 units/mg protein
mol wt
33 kDa
foreign activity
DNase, RNase, none detected
storage temp.
−20°C
General description
Thermitase from Bacillus cereus is a protease that inactivates Rnases, Dnases and enzymes in reactions.
Application
Thermitase is used for the isolation of RNA and DNA (plasmid and genomic). Thermitase has been used in a study to assess the development and application of 15N-tracer substances for measuring the whole-body protein turnover rates. [1] Thermitase has also been used in a study to investigate a computational procedure for transferring a binding site onto an existing protein scaffold. [2]
Biochem/physiol Actions
Thermitase is a thermostable (4-60°C) serine protease that remains active over a wide pH range of 4-12.5. This protease retains its activity in the presence of EDTA, SDS, or Triton™ X-100.
Unit Definition
One unit is defined as the amount of enzyme required to solubilize 1 absorbance unit (595nm) of milk in 60 minutes at 37°C in a total reaction volume of 200ul.
Physical form
Supplied as a solution in 20mM Tris-HCl (pH 7.4), 1mM CaCl2 and 50% glycerol.
Legal Information
Triton is a trademark of The Dow Chemical Company or an affiliated company of Dow
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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OptGraft: A computational procedure for transferring a binding site onto an existing protein scaffold
Fazelinia, H., et al.
Protein Science, 18, 180-195 (2008)
Klaus D Wutzke
Isotopes in environmental and health studies, 48(2), 239-258 (2012-03-09)
Our research group of the Children's Hospital of the University of Rostock (Rostock group) has long-time experience in (15)N-labelling and in using yeast protein and its hydrolysates for tracer kinetic studies to evaluate parameters of the whole-body protein metabolism in
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