luciferase

Luciferase is a flavin-dependent monooxygenase found in bioluminescent bacteria. Luciferase is an invaluable tool for identifying and characterizing functional variants, allowing investigations of gene expression, intracellular signaling, transcription factors, receptor activity, and protein folding.

Luciferase, firefly, is the enzyme responsible for the bioluminescence of fireflies and click beetles. The enzyme catalyzes the oxidation of firefly luciferin, requiring oxygen and ATP.

Hsp70-derived octapeptide acetate (Hsp70-derived octapeptide acetate) is a group of tetratricopeptide repeat (TPR)-containing proteins has been shown to interact with the C-terminal domain of the 70 kDa heat-shock cognate protein (hsc70). In the present study, the effect of the TPR-containing proteins, including the C-terminus of hsc70-interacting protein (CHIP), TPR1 and human glutamine-rich TPR-containing protein (hSGT), on refolding of luciferase by DnaJ and hsc70 was investigated.

A group of tetratricopeptide repeat (TPR)-containing proteins has been shown to interact with the C-terminal domain of the 70 kDa heat-shock cognate protein (hsc70). In the present study, the effect of the TPR-containing proteins, including the C-terminus

[Ala28]-β Amyloid(25-35) (β(25-35)KA), an electrically neutral mutant variant of Aβ(25-35), facilitates the accelerated aggregation of Firefly Luciferase [1].

CT-08 (CT8, Compound 3) is a macrolide Sec61 modulator that inhibits protein secretion in a signal sequence-dependent manner. It prevents the Sec61-mediated translocation of VCAMss-GLuc to the ER, resulting in the loss of luciferase activity. Additionally, CT-08 suppresses the expression of VCAM in transfected cells.