Palmitoyl-Protein Thioesterase 1 (PPT1) Antibody (HRP)

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Description
PPT1 Antibody (HRP) is a Rabbit Polyclonal against PPT1 conjugated to HRP.
Documents del producto
Product specifications
Category | Primary Antibodies |
Immunogen Target | Palmitoyl-Protein Thioesterase 1 (PPT1) |
Host | Rabbit |
Reactivity | Human |
Recommended Dilution | Optimal dilutions/concentrations should be determined by the end user. |
Clonality | Polyclonal |
Conjugation | HRP |
Isotype | IgG |
Purity | > 95% |
Purification | Purified by Protein G. |
Size 1 | 20 µg |
Size 2 | 50 µg |
Size 3 | 100 µg |
Size 4 | 200 µg |
Size 5 | 1 mg |
Form | Liquid |
Tested Applications | ELISA |
Buffer | 0.01 M PBS, pH 7.4, 0.03% Proclin-300 and 50% Glycerol. |
Availability | Shipped within 5-10 working days. |
Storage | Aliquot and store at -20°C. Avoid exposure to light. Avoid repeated freeze/thaw cycles. |
Dry Ice | No |
UniProt ID | P50897 |
Gene ID | 5538 |
NCBI Accession | NP_000301.1, NM_000310.3 |
OMIM | 256730 |
Background | Antibody anti-PPT1 |
Status | RUO |
Descripción
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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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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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