gsh

L-Glutathione reduced (Glutathione) is a naturally occurring tripeptide found in cells as an endogenous antioxidant that scavenges oxygen free radicals. L-Glutathione reduced is a cofactor for certain enzymes and is involved in the rearrangement of protein disulfide bonds and the reduction of peroxides.

Glutathione can occur in reduced (GSH), oxidized (GSSG), or in mixed disulfide forms and is ubiquitous in multiple biological systems serving as the major thiol-disulfide redox buffer of the cell. GSSG is the oxidized form of GSH . It can be reduced back to GSH through the NADPH-dependent enzyme glutathione reductase. GSSG functions as a hydrogen acceptor in the enzymatic determination of NADP+ and NADPH and can be a proximal donor in S-glutathionylation post translational modifications. The ratio of reduced glutathione to oxidized glutathione within cells is often used as an indicator of oxidative stress, with higher concentrations of GSSG predicting increased oxidative stress.

Glutathione ethyl ester TFA is a glutathione substitute and a cell-permeable glutathione GSH donor that modulates age-related oxidative damage in bovine oocytes, improves the developmental capacity of oocytes from aged cows, and prevents early asthma.

Phoenixin-14 TFA (PNX-14) is a blood-brain barrier (BBB)-penetrable neuropeptide with anxiolytic, cardioprotective, and neuroprotective properties. It modulates pituitary gonadotrophin release by enhancing gonadotropin-releasing hormone (GnRH) receptor mRNA expression and promotes insulin secretion. Additionally, PNX-14 TFA protects against ischemia/reperfusion (IR) injury in mice and combats oxidative stress by diminishing reactive oxygen species (ROS) and elevating glutathione (GSH) levels [1] [2] [3].