[6] The renalase protein consists of a putative secretory signal peptide (SignalP score of 0.4), a flavin adenine dinucleotide (FAD)-binding region, and an oxidase domain.

[7] Dr. Gary Desir's laboratory at Yale School of Medicine discovered and named renalase in 2005[6] suggest that the human kidney releases this protein into the bloodstream to regulate blood pressure (in addition to other possible, as yet undiscovered, functions).

In 2013, renalase was claimed to oxidize α-NADH (the normal form of NADH is the β anomer) to β-NAD+, with concomitant reduction of O2 (dioxygen) to H2O2 (hydrogen peroxide).

[11] This reaction was proposed to repair aberrant NADH and NADPH forms that are not accepted as cofactors by most nicotinamide-dependent oxidoreductase enzymes.

The renalase flavin then delivers the electrons harvested to O2 (dioxygen) forming H2O2 (hydrogen peroxide), completing the catalytic cycle.

[11] In contrast to clear evidence for catalysis of this activity, the native renalase used in these experiments did not catalyze the conversion of the catecholamine epinephrine to adrenochrome.

[14] The binding of renalase to PMCA4b stimulates calcium efflux with subsequent activation of the PI3K and MAPK pathways, increased expression of the anti-apoptotic factor Bcl-2, and decreased caspase3-mediated apoptosis.

Administration of recombinant renalase protects against acute kidney injury (AKI), and against cardiac ischemia in animal models.

When catecholamines are released into the bloodstream however, renalase activity increases about tenfold within 30 seconds, and remains high for an hour or longer.