Detection, isolation and uses of renalase (monoamine oxidase C)

1. A method for producing renalase protein capable of metabolizing catecholamines, comprising, synthesizing recombinant renalase protein in a host cell in the presence of flavin adenine dinucleotide (FAD), and recovering the renalase protein;

wherein the renalase protein comprises an FAD-binding site and an amine oxidase domain, and comprises an amino acid sequence having at least 90% sequence identity to SEQ ID NO:2.

2. The method of claim 1 , wherein the renalase protein comprises an amino acid sequence having at least 95% sequence identity to SEQ ID NO:2.

3. The method of claim 1 , wherein the renalase protein comprises the amino acid sequence of SEQ ID NO:2.

4. The method of claim 1 , wherein the renalase protein comprises an amino acid sequence encoded by SEQ ID NO:1 or SEQ ID NO:3.

5. The method of claim 1 , wherein the catecholamine is dopamine, epinephrine, or norepinephrine.

6. The method of claim 1 , wherein the host cell is a bacterial, yeast, insect, or vertebrate host cell.

7. The method of claim 6 , wherein the host cell is E. coli.

8. The method of claim 6 , wherein the host cell is a yeast.

9. The method of claim 6 , wherein the host cell is mammalian.

10. The method of claim 1 , wherein FAD is added at the time of inducing protein synthesis.

11. The method of claim 1 , wherein the renalase protein comprises a purification tag.

12. The method of claim 11 , wherein the purification tag is glutathione-S-transferase (GST), maltose binding protein (MBP), influenza virus hemaglutinin (HA), HIS 6 , or FLAG.

13. The method of claim 1 , wherein the renalase protein is recovered by affinity chromatography.

14. The method of claim 1 , wherein the renalase protein is further denatured and refolded.

15. The method of claim 14 , wherein the renalase protein is recovered in inclusion bodies, denatured with urea, and refolded.