Analytical Data
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Gene name
PPM1D
- Application
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Alternative Names
PP2C-DELTA; WIP1; Wild-Type p53-Induced Phosphatase 1; Protein Phosphatase 2C,Delta Isoform; Protein Phosphatase 1D Magnesium-Dependent,Delta
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O15297
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Expression Region
Ser400-Cys605
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Molecular Weight
30kDa
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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
Related Products
Protein Description
PPM1D, also known as Protein Phosphatase, Magnesium-dependent 1D, is a serine/threonine phosphatase that plays a pivotal role in various cellular processes, including cell cycle regulation, DNA damage response, and apoptosis. Dysregulation of PPM1D has been implicated in several cancers, particularly those associated with mutations in the p53 tumor suppressor pathway. Research indicates that PPM1D acts as a negative regulator of the p53 pathway, promoting tumorigenesis by dephosphorylating key substrates involved in cellular stress responses. Studies have shown that PPM1D is overexpressed in various human cancers, and its inhibition can sensitize cancer cells to chemotherapy and radiotherapy. This has led to increased interest in developing PPM1D as a potential therapeutic target. The production of recombinant PPM1D protein enables detailed biochemical analysis and the exploration of its functional interactions with other cellular molecules. Understanding the mechanisms that underpin PPM1D's role in cancer biology is crucial for identifying novel therapeutic strategies and improving treatment outcomes for patients with PPM1D-related malignancies. The ongoing research into PPM1D is therefore not only significant for elucidating its basic biological functions but also for its potential applications in cancer therapeutics.
