Thimet Oligopeptidase from Bacillus licheniformis

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.

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.

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.