Analytical Data
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Gene name
PPT1
- Application
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Alternative Names
PPT1；CLN1；Palmitoyl-Protein thioesterase 1
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Species
Human
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Source
E. coli
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Tag
N-terminal His Tag
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P50897
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Expression Region
28~306aa
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AA Sequence
DPPAPLPLVIWHGMGDSCCNPLSMGAIKKMVEKKIPGIYVLSLEIGKTLMEDVENSFFLNVNSQVTTVCQALAKDPKLQQGYNAMGFSQGGQFLRAVAQRCPSPPMINLISVGGQHQGVFGLPRCPGESSHICDFIRKTLNAGAYSKVVQERLVOAEYWHDPIKEDVYRNHSIFLADINQERGINESYKKNLMALKKFVMVKFLNDSIVDPVDSEWFGFYRSGQAKETIPLQETSLYTQDRLGLKEMDNAGQLVFLATEGDHLQLSEEWFYAHIIPFLG
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Molecular Weight
35.0kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
Reconstitute in 20mM Tris, 150mM NaCl (pH8.0) to a concentration of 0.1-1.0 mg/mL. Do not vortex.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Identification
Protein Description
The study of PPT1 (palmitoyl-protein thioesterase 1) has garnered considerable attention due to its crucial role in various biological processes and its implications in human health, particularly in neurodegenerative diseases. PPT1 is a lysosomal enzyme responsible for the removal of palmitoyl groups from proteins, a post-translational modification that plays a significant role in regulating protein function, stability, and subcellular localization. Mutations in the PPT1 gene are linked to the rare neurodegenerative disorder, CLN1 disease (classical late-infantile neuronal ceroid lipofuscinosis), which is characterized by progressive cognitive decline, loss of motor skills, and premature death. Research has shown that impaired PPT1 function leads to the accumulation of palmitoylated proteins, contributing to lysosomal dysfunction and neuronal degeneration. Understanding the mechanism of PPT1 and its role in protein modification is essential for developing potential therapeutic strategies aimed at mitigating the effects of CLN1 and other related disorders. Furthermore, ongoing studies into PPT1’s enzymatic activity and its interactions with various substrates may provide insights into broader applications in biotechnology and protein engineering, highlighting the enzyme's significance beyond neurobiology. With advances in structural biology and protein engineering techniques, further elucidation of PPT1's function could pave the way for novel interventions in lipid metabolism disorders and enhance our understanding of cellular degradation processes. As research continues to unfold, the exploration of PPT1 remains a dynamic field that bridges basic science and potential clinical applications.
