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T7705

Thimet Oligopeptidase from Bacillus licheniformis

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UNSPSC Code:
12352204
NACRES:
NA.54
Número CE:
Form:
powder
Storage temp.:
−20°C
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recombinant

expressed in E. coli

Quality Level

form

powder

mol wt

~77 kDa

storage temp.

−20°C

Categorías relacionadas

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.

pictograms

Exclamation mark

signalword

Warning

hcodes

Hazard Classifications

Acute Tox. 4 Inhalation - Skin Irrit. 2

Clase de almacenamiento

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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Fernanda M Cunha et al.
The Journal of biological chemistry, 283(36), 24448-24459 (2008-07-12)
Protein degradation by the ubiquitin proteasome system releases large amounts of oligopeptides within cells. To investigate possible functions for these intracellularly generated oligopeptides, we fused them to a cationic transactivator peptide sequence using reversible disulfide bonds, introduced them into cells
Kirsty Cleverly et al.
Reproduction (Cambridge, England), 139(2), 319-330 (2009-09-17)
LHRH (GNRH) was first isolated in the mammalian hypothalamus and shown to be the primary regulator of the reproductive neuroendocrine axis comprising of the hypothalamus, pituitary and gonads. LHRH acts centrally through its initiation of pituitary gonadotrophin release. Since its
Lisa A Bruce et al.
Neuropeptides, 46(4), 167-172 (2012-06-08)
Thimet oligopeptidase (TOP) and prolyl endopeptidase (PEP) are neuropeptidases involved in the hydrolysis of gonadotropin-releasing hormone, a key component of the hypothalamic-pituitary-gonadal axis. GnRH is regulated in part by feedback from steroid hormones such as estradiol. Previously, we demonstrated that
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
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

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SKUGTIN
T7705-100UN04061831160314

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