The glutathione shunt is one of the most important contributors to cellular redox state, with implications across cancer, chronic and diseases of ageing, and autoimmune diseases. Traditionally, the redox state is gauged by the ratio of the metabolites GSH and GSSG. However, this presents methodological challenges without a systems-level understanding of redox dynamics. Targeted proteomics can fill this void. A novel in-parallel metabolomic and proteomic targeted method has been developed. Samples are simultaneously prepared to extract the substrate building blocks, cysteine, cystine, methionine, glutamic acid, and kynurenine; and the proteins, SLC7A11 (xCT), glutamate cysteine ligase (modifier subunit GSH0 and catalytic subunit GSH1), glutathione synthetase (GSH2), glutathione peroxidase (GPx), and glutathione reductase (GSHR) for targeted mass spectrometry. This multi-omics method can provide an elegant snapshot of the redox state from the same patient, at the same time-point, from the same sample for both enzymes and metabolites that extends beyond the requirement for cellular / tissue extracts. This allows for a broader narrative to establish context at which redox is operating.