Recombinant Human PPT1 HA-tag His-tag Protein, CF New

Scientific Data

Recombinant human palmitoyl-protein thioesterase 1 (PPT1), also known as CLN1, is one of two PPT lysosomal thioesterase proteins that catalyze the hydrolysis of long-chain fatty acids (1, 2). While the two PPT enzymes share 18% identity and some overlap in functionality, their specificities differ; PPT1 is the key enzyme responsible for catalyzing the removal of palmitate from S-palmitoylated proteins to facilitate their degradation and clearance from the lysosome (2-4). PPT1 is a glycosylated, monomeric protein that contains a signal peptide, a canonical alpha / beta -hydrolase fold, a catalytic triad, and a fatty-acid hydrophobic groove binding site for palmitate (4). Mutations in PPT1 resulting in defects in activity lead to accumulation of lipid-modified proteins and cause fatal neurodegenerative lysosomal storage disorders known as neuronal ceroid lipofuscinoses (NCL) or Batten disease (4-6).  As PPT1 plays a regulatory role in the autophagy-lysosome pathway, it is also a target for several types of cancer including hepatic, melanoma, and oral squamous cell carcinoma (7-10). Pharmacological methods for targeting of PPT1 via gene therapy, enzyme replacement therapy, or enzymatic-related inhibition are under investigation for the treatment of both NCLs and cancer (7, 8,11-13).