Analytical Data
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Gene name
PPT2
- Application
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Alternative Names
PPT2Lysosomal thioesterase PPT2; PPT-2; EC 3.1.2.-; S-thioesterase G14
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9UMR5
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Expression Region
28-302 aa
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AA Sequence
APA PHRASYKPVI VVHGLFDSSY SFRHLLEYIN ETHPGTVVTV LDLFDGRESL RPLWEQVQGF REAVVPIMAK APQGVHLICY SQGGLVCRAL LSVMDDHNVD SFISLSSPQM GQYGDTDYLK WLFPTSMRSN LYRICYSPWG QEFSICNYWH DPHHDDLYLN ASSFLALING ERDHPNATVW RKNFLRVGHL VLIGGPDDGV ITPWQSSFFG FYDANETVLE MEEQLVYLRD SFGLKTLLAR GAIVRCPMAG ISHTAWHSNR TLYETCIEPW LS
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Molecular Weight
34.2 kDa
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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
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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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
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Protein Description
PPT2, or Protein Phosphatase 2, is a crucial enzyme involved in various cellular signaling pathways by dephosphorylating proteins, thereby regulating their activity. The research surrounding PPT2 has gained significant attention due to its potential implications in health and disease. Aberrant regulation of protein phosphorylation is often linked to various conditions, including cancer, neurodegenerative diseases, and metabolic disorders. Understanding the structure and function of PPT2 can provide insights into mechanisms of disease progression and aid in the development of therapeutic strategies. Recent studies have focused on the recombinant expression of PPT2 to enable detailed biochemical and structural analyses. By producing PPT2 in a controlled environment, researchers can investigate its enzymatic properties, substrate specificity, and interaction with other regulatory proteins. Moreover, dissecting the role of PPT2 in specific physiological processes may reveal novel pathways for therapeutic intervention. The exploration of PPT2 not only enhances our knowledge of protein phosphatases but also serves as a foundation for potential drug discovery efforts aimed at modulating its activity in disease contexts. As such, PPT2 represents a vital area of research within the broader field of cellular signaling and molecular biology.
