CTH, also named as Gamma-cystathionase and CSE, belongs to the transsulfuration enzymes family. It catalyzes the last step in the transsulfuration pathway from methionine to cysteine. CTH has broad substrate specificity. It converts cystathionine to cysteine, ammonia and 2-oxobutanoate. And it converts two cysteine molecules to lanthionine and hydrogen sulfide. CTH can also accept homocysteine as substrate. It specificity depends on the levels of the endogenous substrates. CTH is the major H2S-producing enzyme in kidney, liver, vascular smooth muscle cells and enterocytes. The endogenous production of H2S plays a significant role in the regulation of cellular functions, including cell growth, hyperpolarization of cell membranes, modulation of neuronal excitability and relaxation of smooth muscle cells. The CSE/H2S pathway is upregulated in the heart in a murine model of CVB3-induced myocarditis and that inhibition of endogenous H2S is beneficial to treatment early in the disease while administration of exogenous H2S is protective to infected myocardium during the later stage. Mutations in the gene encoding CTH can result in the autosomal recessive disease cystathioninuria; a disorder characterized by the unusual accumulation of plasma cystathionine causing increased urinary excretion. Both male and female CTH-null mice showed hypercystathioninemia and hyperhomocysteinemia, but not hypermethioninemia. CSE has also been reported to be expressed in endothelial cells and contribute to endothelium-dependent vasorelaxation. This antibody is a rabbit polyclonal antibody raised against residues near the C terminus of human CTH.