Rat Palmitoyl-Protein Thioesterase 1 (PPT1) ELISA Kit

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Description
Rat Palmitoyl-Protein Thioesterase 1 (PPT1) ELISA Kit is an ELISA Kit for the in vitro quantitative measurement of Rat Palmitoyl-protein thioesterase 1 concentrations in serum, plasma, tissue homogenates, cell lysates and other biological fluids.
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Product specifications
Category | ELISA Kits |
Immunogen Target | Palmitoyl-Protein Thioesterase 1 (PPT1) |
Reactivity | Rat |
Detection Method | Colorimetric |
Assay Data | Quantitative |
Assay Type | Sandwich |
Test Range | 0.625 ng/ml - 40 ng/ml |
Sensitivity | < 0.312 ng/ml |
Recommended Dilution | Optimal dilutions/concentrations should be determined by the end user. |
Size 1 | 96 tests |
Form | Lyophilized |
Tested Applications | ELISA |
Sample Type | Serum, plasma, tissue homogenates, cell lysates and other biological fluids. |
Availability | Shipped within 1-3 weeks. The validity for this kit is 6 months. |
Storage | Shipped at 4 °C. Upon receipt, store the kit according to the storage instruction in the kit's manual. |
Dry Ice | No |
UniProt ID | P45479 |
Background | Elisa kits for PPT1 |
Status | RUO |
Note | Validity: The validity for this kit is 6 months. This product is for research use only. The range and sensitivity is subject to change. Please contact us for the latest product information. For accurate results, sample concentrations must be diluted to mid-range of the kit. If you require a specific range, please contact us in advance or write your request in your order comments. Please note that our ELISA and CLIA kits are optimised for detection of native samples, rather than recombinant proteins. We are unable to guarantee detection of recombinant proteins, as they may have different sequences or tertiary structures to the native protein. |
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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