PPT1 (human, recombinant)

Palmitoyl-protein thioesterase 1 (PPT1) is a lysosomal hydrolase involved in removing palmitic acid (Cay-10006627) from post-translationally modified proteins prior to their degradation. It is mainly expressed in the brain but is also found in visceral macrophages from liver, lung, and bowel tissues. PPT1 depalmitoylates proteins in cells undergoing autophagy, and PPT1 activity is important for axon outgrowth, neurite extension, and dendritic spine morphology. Knockout of PPT1 decreases tumor growth in a mouse xenograft model, and high expression of PPT1 is associated with poor overall survival in several cancers. Mutations in PPT1 cause infantile neuronal ceroid lipofuscinoses (INCL), an encephalopathy characterized by granular deposits in neurons, vision loss, seizures, mental deterioration, and brain death. Cayman's PPT1 (human, recombinant) protein consists of 290 amino acids, has a calculated molecular weight of 32.7 kDa, and a predicted N-terminus of Asp28 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass is 35-41 kDa due to glycosylation.Synonyms: Palmitoyl-protein Hydrolase 1, Palmitoyl-protein Thioesterase 1, CLN1. Purity: >90% estimated by SDS-PAGE. Endotoxin Testing: <1.0 EU/µg determined by the LAL endotoxin assay. Source: Recombinant human C-terminal His-tagged PPT1 expressed in HEK293 cells. Amino Acids: 28-306. MW: 32.7 kDa. Formulation: (Request formulation change), Lyophilized from sterile PBS, pH 7.4. UniProt Accession #: P50897-1.