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PPT1 Mouse anti-Canine, Human, Non-human primate, Clone: OTI1A10, Invitrogen™

Mouse Monoclonal Antibody

Manufacturer:  Invitrogen MA526457

Catalog No. PIMA526457

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Palmitoyl-protein thioesterase-1 (PPT1) is a lysosomal hydrolase that removes long-chain fatty acyl groups from modified cysteine residues in proteins. Mutations in PPT1 have been found to cause the infantile form of neuronal ceroid lipofuscinosis (INCL), and an animal model has been developed.1 The deduced PPT2 protein contains 302 amino acids, including a 27-amino acid leader peptide, a sequence motif characteristic of many thioesterases and lipases, and 5 potential N-linked glycosylation sites.2 PPT2 shares 18% amino acid identity with PPT1. Northern blot analysis detected a predomit 2.0-kb PPT2 transcript in the human tissues examined, with the highest expression in skeletal muscle; variable amounts of 2.8- and 7.0-kb transcripts were also observed. Recombit PPT2, like PPT1, possesses thioesterase activity and localizes to the lysosome. Since PPT2 could not substitute for PPT1 in correcting the metabolic defect in INCL cells and was unable to remove palmitate groups from palmitoylated proteins that are routinely used as substrates for PPT1it has been postulated that PPT2 possesses a different substrate specificity than PPT1.


1 mg/mL
PBS with 1% BSA, 50% glycerol and 0.02% sodium azide; pH 7.3
P50897, Q8HXW6
CLN1, INCL, PPT, PPT-1, ceroid-palmitoyl-palmitoyl-protein thioesterase 1, palmitoyl-protein hydrolase 1
100 μL
-20° C, Avoid Freeze/Thaw Cycles
102126191, 475316, 5538
Immunohistochemistry (Paraffin), Western Blot
Human recombit protein fragment corresponding to amino acids 100-306 of PPT1 produced in E.coli
Affinity Chromatography
Canine, Human, Non-human primate
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