Human N-fatty-acryl-amino acid synthase/hydrolase PM20D1 gene encodes a bidirectional N-fatty-acyl amino acid synthase/hydrolase that regulates the production of N-fatty-acyl amino acids. These metabolites are endogenous chemical uncouplers of mitochondrial respiration. In an UCP1-independent manner, maybe through interaction with mitochondrial transporters, they promote proton leakage into the mitochondrial matrix. Thereby, this secreted protein may indirectly regulate the bodily dissipation of chemical energy as heat through thermogenic respiration.

Full-length mature protein of human PM20D1 cDNA (26-502aa) was constructed with codon optimization gene synthesis technology and expressed with a small T7-His-TEV cleavage site Tag (29aa) fusion at its N-terminal. This protein was expressed in E. coli as inclusion bodies. The final product was refolded using our unique “temperature shift inclusion body refolding” technology and chromatographically purified.

1. May be used for in vitro PM20D1 mediated adipocyte mitochondrial respiratory activities regulation study in N-acyl amino acids metabolizing signaling pathway with this protein either as soluble factor or as coating matrix protein.

2. May be used for protein-protein interaction assay.

3. May be used as enzymatic substrate for various proteases assay.

4. Potential therapeutic protein for regulating adipocytes metabolic pathway in vivo for treatment of diabetes.

5. As immunogen for specific antibody production.