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T7705

Thimet Oligopeptidase from Bacillus licheniformis

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100 units
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₪1,686.00

About This Item

UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
Form:
powder
Storage temp.:
−20°C

₪1,686.00


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recombinant

expressed in E. coli

Quality Level

form

powder

mol wt

~77 kDa

storage temp.

−20°C

General description

Thimet oligopeptidase is considered essential in the degradation of collagen in collaboration with collagenolytic enzymes. Thimet oligopeptidase (TOP) is a neuropeptidase involved in the hydrolysis of gonadotropin-releasing hormone, a key component of the hypothalamic-pituitary-gonadal axis. [1]

Application

Thimet oligopeptidase can be used for the degradation of collagen in combination with collagenases. It can also be used for the hydrolysis of neuropeptides such as bradykin, neurotensin, and amyliod-β-peptide. Thimet oligopeptidase has been used in a study to investigate the effect of acute cocaine administration in male rats on TOP specific activity and mRNA levels in prosencephalic brain areas related with the reward circuitry: ventral striatum, hippocampus, and frontal cortex. [2]

Preparation Note

This enzyme has been affinity chromatographically purified using a niquel affinity column. It contains a 6-Histidine tag in its C-terminus.

A working solution of this enzyme can be prepared in 20 mM phosphate buffered saline solution, pH 7.0, or sterile and deionized water, pH 7.0.

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P5459A3403O9515
Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200

form

powder

form

glycerol solution (50%)

form

saline solution

form

solution

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

−70°C

mol wt

~77 kDa

mol wt

-

mol wt

57.6 kDa

mol wt

81.6 kDa

recombinant

expressed in E. coli

recombinant

-

recombinant

-

recombinant

expressed in E. coli


pictograms

Exclamation mark

signalword

Warning

hcodes

Hazard Classifications

Acute Tox. 4 Inhalation - Skin Irrit. 2

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable



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Lilian C Russo et al.
Proteomics, 12(17), 2641-2655 (2012-06-29)
Protein interactions are crucial for most cellular process. Thus, rationally designed peptides that act as competitive assembly inhibitors of protein interactions by mimicking specific, determined structural elements have been extensively used in clinical and basic research. Recently, mammalian cells have
Akio Kawasaki et al.
The Journal of biological chemistry, 285(45), 34972-34980 (2010-09-08)
Pz-peptidase A, from the thermophilic bacterium Geobacillus collagenovorans MO-1, hydrolyzes a synthetic peptide substrate, 4-phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-D-Arg (Pz-PLGPR), which contains a collagen-specific tripeptide sequence, -Gly-Pro-X-, but does not act on collagen proteins themselves. The mammalian enzyme, thimet oligopeptidase (TOP), which has comparable
T John Wu et al.
Journal of neuroendocrinology, 21(4), 293-298 (2009-02-13)
Gonadotrophin-releasing hormone (GnRH) was first isolated in the mammal and shown to be the primary regulator of the reproductive system through its initiation of pituitary gonadotrophin release. Subsequent to its discovery, this form of GnRH has been shown to be



Global Trade Item Number

SKUGTIN
T7705-100UN04061831160314

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