Human Palmitoyl-Protein Thioesterase 1 (PPT1) Protein
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Description
Palmitoyl-Protein Thioesterase 1 (PPT1) protein is a recombinant Human protein expressed in HEK293 cells.
Documents del producto
Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | Palmitoyl-Protein Thioesterase 1 (PPT1) |
| Host | HEK293 cells |
| Assay Type | Activity: Not tested Sequence Fragment: Asp28-Gly306 Tag: C-terminal 6 His tag |
| Origin | Human |
| Observed MW | Calculated MW: 32.3 kDa Observed MW (SDS-PAGE): 34-41 kDa |
| Expression | Recombinant |
| Purity | > 90% (SDS-PAGE) |
| Purification | 0.2 µm filtered. |
| Size 1 | 10 µg |
| Size 2 | 50 µg |
| Form | Liquid |
| Tested Applications | SDS-PAGE |
| Buffer | 20 mM Tris-HCl, 150 mM NaCl, pH 7.4 containing 10% Glycerol. |
| Availability | Shipped within 5-15 working days. |
| Storage | Aliquot and store at -20 °C. Avoid repeated freeze/thaw cycles. Shelf Life: 6 months. |
| Dry Ice | No |
| UniProt ID | P50897 |
| Gene ID | 5538 |
| OMIM | 256730, 600722 |
| Background | Protein PPT1 |
| Status | RUO |
| Note | THIS PRODUCT IS FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC, THERAPEUTIC OR COSMETIC PROCEDURES. NOT FOR HUMAN OR ANIMAL CONSUMPTION. Endotoxin Level: < 1.0 EU per µg (LAL method). |
Descripción
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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 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.
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