T7705
Thimet Oligopeptidase from Bacillus licheniformis
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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.
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.
Signal Word
Warning
Hazard Statements
Precautionary Statements
Hazard Classifications
Acute Tox. 4 Inhalation - Skin Irrit. 2
Storage Class Code
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
Denis Ravel et al.
Clinical cancer research : an official journal of the American Association for Cancer Research, 14(4), 1258-1265 (2008-02-19)
There is a clear clinical need for cytotoxic drugs with a lower systemic toxicity. DTS-201 (CPI-0004Na) is a peptidic prodrug of doxorubicin that shows an improved therapeutic index in experimental models. The purpose of the current study was to complete
Maurício F M Machado et al.
Biochemical and biophysical research communications, 394(2), 429-433 (2010-03-17)
Thimet oligopeptidase (EC 3.4.24.15, TOP) is a metallo-oligopeptidase that participates in the intracellular metabolism of peptides. Predictions based on structurally analogous peptidases (Dcp and ACE-2) show that TOP can present a hinge-bend movement during substrate hydrolysis, what brings some residues
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