T7902

Thermolysin from Geobacillus stearothermophilus

Name: Thermolysin from <I>Geobacillus stearothermophilus</I>
Brand: SIGMA

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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All Photos(1)

About This Item

CAS Number:

9073-78-3

UNSPSC Code:

12352204

NACRES:

NA.75

EC Number:

232-973-4

MDL number:

MFCD00165549

EC Number:

3.4.24.27 (BRENDA, IUBMB)

Product Name

Thermolysin from Geobacillus stearothermophilus, powder, BioReagent, 30-350 units/mg protein (E1%/280), suitable for cell culture

biological source

Geobacillus stearothermophilus

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

Quality Level

200

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Related Categories

Cell Culture & Analysis

Cell Culture Supplements & Reagents

Cell Dissociation Reagents

Molecular Biology & Functional Genomics

Protein Biology

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.

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).

Physical form

lyophilized powder containing calcium and sodium acetate buffer salts

pictograms

GHS08

signalword

Danger

hcodes

H334

pcodes

P261 - P284 - P501

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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

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Single-Cell Transcriptomes Reveal a Complex Cellular Landscape in the Middle Ear and Differential Capacities for Acute Response to Infection.

Allen F Ryan et al.

Frontiers in genetics, 11, 358-358 (2020-05-01)

Single-cell transcriptomics was used to profile cells of the normal murine middle ear. Clustering analysis of 6770 transcriptomes identified 17 cell clusters corresponding to distinct cell types: five epithelial, three stromal, three lymphocyte, two monocyte, two endothelial, one pericyte and

GRID-based three-dimensional pharmacophores I: FLAPpharm, a novel approach for pharmacophore elucidation.

Simon Cross et al.

Journal of chemical information and modeling, 52(10), 2587-2598 (2012-09-14)

Pharmacophore elucidation approaches are routinely used in drug discovery, primarily with the aim of determining the three-dimensional arrangement of common features shared by ligands interacting at the site of interest; these features can then be used to investigate the structure-activity

Nanoflow electrospinning serial femtosecond crystallography.

Raymond G Sierra et al.

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

Effects of site-directed mutagenesis in the N-terminal domain of thermolysin on its stabilization.

Yuichi Kawasaki et al.

Journal of biochemistry, 153(1), 85-92 (2012-10-23)

The thermolysin variant G8C/N60C/S65P in which the triple mutation in the N-terminal domain, Gly8→Cys/Asn60→Cys/Ser65→Pro, is undertaken increases stability [Yasukawa, K. and Inouye, K. (2007) Improving the activity and stability of thermolysin by site-directed mutagenesis. Biochim. Biophys. Acta 1774, 1281-1288] and

LC-MS/MS coupled with QSAR modeling in characterising of angiotensin I-converting enzyme inhibitory peptides from soybean proteins.

Yuchen Gu et al.

Food chemistry, 141(3), 2682-2690 (2013-07-23)

The importance of soy products in reducing the risk of cardiovascular disease is well documented. Our previous computation study has indicated the presence of several potent ACE inhibitory peptides within soybean proteins which needs to be identified. The aim of

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