|Application ||WB, E|
|Other Accession||Q8HXW6, P45478|
|Calculated MW||34193 Da|
|Antigen Region||32-63 aa|
|Other Names||Palmitoyl-protein thioesterase 1, PPT-1, Palmitoyl-protein hydrolase 1, PPT1, PPT|
|Target/Specificity||This PPT1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 32-63 amino acids from the N-terminal region of human PPT1.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||PPT1 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Removes thioester-linked fatty acyl groups such as palmitate from modified cysteine residues in proteins or peptides during lysosomal degradation. Prefers acyl chain lengths of 14 to 18 carbons.|
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Provided below are standard protocols that you may find useful for product applications.
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 predominant 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. Recombinant 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.
Calero, G., et al., J. Biol. Chem. 278(39):37957-37964 (2003).
Hofmann, S.L., et al., Curr. Mol. Med. 2(5):423-437 (2002).
Weimer, J.M., et al., Neuromolecular Med. 1(2):111-124 (2002).
Lu, J.Y., et al., Proc. Natl. Acad. Sci. U.S.A. 93(19):10046-10050 (1996).
Crews, C.M., et al., Proc. Natl. Acad. Sci. U.S.A. 93(9):4316-4319 (1996).
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