Recombinant Mouse Palmitoyl-Protein Thioesterase 1 (PPT1) Protein (His)

Beta LifeScience SKU/CAT #: BLC-00249P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Mouse Palmitoyl-Protein Thioesterase 1 (PPT1) Protein (His)

Beta LifeScience SKU/CAT #: BLC-00249P
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Product Overview

Description Recombinant Mouse Palmitoyl-Protein Thioesterase 1 (PPT1) Protein (His) is produced by our Mammalian cell expression system. This is a protein fragment.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb O88531
Target Symbol PPT1
Species Mus musculus (Mouse)
Expression System Mammalian cell
Tag C-10His
Target Protein Sequence DPPSPPPLVIWHGMGDSCCNPMSMGVIKKMVEKEIPGIYVLSLEIGKNMMEDVENSFFLNVNVQVNMVCQILEKDPKLQQGYNAIGFSQGGQFLRAVAQRCPTPPMMTLISVGGQHQGVFGLPRCPGESSHICDFIRKSLNAGAYSKLVQERLVQAQYWHDPIKESVYRNYSIFLADINQERCVNESYKKNLMALKKFVMVKFFNDSIVDPVDSEWFGFYRSGQAKETIPLQESTLYTEDRLGLKKMDKAGKLVFLAKEGDHLQISKEWFTAHIIPFLK
Expression Range 28-306aa
Protein Length Partial
Mol. Weight 33.0 kDa
Research Area Others
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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.
Subcellular Location Lysosome. Secreted.
Protein Families Palmitoyl-protein thioesterase family
Database References

KEGG: mmu:19063

STRING: 10090.ENSMUSP00000030412

UniGene: PMID: 27722792

  • Proteomics analysis on isolated cilia revealed 660 proteins, which differed in their abundance levels between wild type and Ppt1 knock out. PMID: 28334871
  • In the novel Cln1(R151X) mouse model of INCL. PMID: 26648046
  • Parkinson-like motor/sensorimotor deficits in Cln1-/- mice are not mediated by dopamine deficiency. PMID: 26238334
  • Data show that Cln1 mutations disrupt the maturation of cathepsin D in lysosome contributing to neuropathology of infantile neuronal ceroid lipofuscinoses and suggest cathepsin D deficiency to be common link between infantile and congenital form. PMID: 26160911
  • The authors have generated a Cln1 R151X point mutation mouse model that recapitulates the molecular, neuropathological and behavioral phenotypes of neuronal ceroid lipofuscinoses. PMID: 25205113
  • Data (including data from knockout mice) suggest that deficiency of Ppt1 leads to accumulation of granular osmiophilic deposits in many cell types, especially in astrocytes. [review-like article] PMID: 25233404
  • Data suggest that mouse macrophages express PPT1; PPT1 appears to contribute to 2-arachidonylglycerol hydrolysis activity in peritoneal macrophages in culture. PMID: 24083319
  • The simultaneous loss of both Cln1 and Cln5 genes might enhance the typical pathological phenotypes of these mice by disrupting or downregulating shared or convergent pathogenic pathways. PMID: 23065637
  • These results uncover a previously unknown phenotype associated with PPT1 deficiency, that of altered thermoregulation, which is associated with impaired lipolysis and neurotransmitter release to brown adipose tissue during cold exposure. PMID: 23139814
  • The addition of the small molecule PPT1 mimetic can further increase that response. PMID: 22310926
  • Glutamate receptor 4 (GluR4) AMPA receptor hypofunction and NMDA receptor hyperfunction phenotype show increased sensitivity in Ppt1-deficient neurons. PMID: 21971706
  • Data show a progressive breakdown of axons and synapses in the brains of two different models of NCL: Ppt1(-/-) model of infantile NCL and Cln6(nclf) model of variant late-infantile NCL. PMID: 19640925
  • The polarized axonal targeting of PPT1 may well indicate a role for PPT1 in the exocytotic pathway of neurons. PMID: 12483688
  • was only detected in developing testis not ovary PMID: 15128596
  • The severely affected PPT1-/- mouse CNS exhibited reduced volume of both cortical and subcortical regions, but with sparing of the cerebellum PMID: 15193291
  • Autopsy of PPT1 mutant mice revealed a severe loss of brain mass and accumulation of autofluorescent granular osmiophilic deposits, both characteristic of Neuronal Ceroid Lipofuscinosis. PMID: 15649713
  • We conclude that from an early age, neurons deficient in PPT1 enzyme activity display intrinsically abnormal properties that could potentially explain key features of the clinical disease, such as myoclonus and seizures. PMID: 16242638
  • Palmitoyl-protein thioesterase-1 deficiency mediates the activation of the unfolded protein response and neuronal apoptosis in infantile neuronal ceroid lipofuscinosis. PMID: 16368712
  • Age-dependent increase in LPC levels in the PPT1-KO mouse brain positively correlates with elevated expression of the genes characteristically associated with phagocytes. PMID: 17341491
  • Neuron-specific changes for F(1)-complex in the Ppt1-deficient cells and give clues for a possible link between lipid metabolism and neurodegeneration in Infantile neuronal ceroid lipofuscinosis. PMID: 18245779
  • We analyzed locus specific gene expression and showed regional clustering of Cln1 and three major genes of this pathway, further supporting a close functional relationship between the corresponding gene products PMID: 18371231
  • Palmitoyl protein thioesterase-1 deficiency impairs synaptic vesicle recycling at nerve terminals in humans and mice PMID: 18704195
  • This study suggests that neuronal-glial interactions are the core pathology in the palmitoyl protein thioesterase 1 deficient cerebellum. PMID: 19416667
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    Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

    Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

    Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

    Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

    To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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