Analytical Data
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Gene name
MDM4
- Application
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Alternative Names
MDM4；MDMX；Protein Mdm4
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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
O15151
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Expression Region
381-490aa
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AA Sequence
ENSKLFDPCNSVEFLDLAHSSESQETISSMGEQLDNLSEQRTDTENMEDC QNLLKPCSLCEKRPRDGNIIHGRTGHLVTCFHCARRLKKAGASCPICKKE IQLVIKVFIA
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Molecular Weight
38 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
Related Products
Protein Description
MDM4, a key regulator in p53 signaling, plays a pivotal role in cellular response to stress and tumorigenesis. Overexpression of MDM4 has been implicated in various cancers, as it negatively regulates p53, an essential tumor suppressor that prevents cell cycle progression and promotes apoptosis in response to DNA damage. Research into MDM4's structure and function has revealed its ability to interact with p53 through a unique mechanism, inhibiting p53's transcriptional activity. Given the challenging nature of targeting protein-protein interactions in drug design, scientists have focused on understanding the molecular details of MDM4's action and how its dysregulation contributes to cancer progression. Recombining MDM4 proteins not only enables the study of their functional properties but also provides insights into potential therapeutic strategies aimed at restoring p53 activity in tumors where MDM4 is overexpressed. This research holds significant promise for developing innovative cancer treatments by targeting the MDM4-p53 axis, potentially leading to more effective interventions for patients with MDM4-related malignancies.
