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AB167941

Recombinant Human MDM2 protein

5

(1 Review)

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(1 Publication)

Recombinant Human MDM2 protein is a Human Fragment protein, in the 1 to 118 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE, WB.

View Alternative Names

E3 ubiquitin-protein ligase Mdm2, Double minute 2 protein, Oncoprotein Mdm2, RING-type E3 ubiquitin transferase Mdm2, p53-binding protein Mdm2, Hdm2, MDM2

1 Images
SDS-PAGE - Recombinant Human MDM2 protein (AB167941)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human MDM2 protein (AB167941)

SDS-Page analysis of ab167941

Key facts

Purity

>85% Densitometry

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE, WB

applications

Biologically active

No

Accession

Q00987

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7 Preservative: 1.02% Imidazole Constituents: 25% Glycerol (glycerin, glycerine), 1.75% Sodium chloride, 0.82% Sodium phosphate, 0.004% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.002% PMSF

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MHHHHHHGSMCNTNMSVPTDGAVTTSQIPASEQETLVRPKPLLLKLLKSVGAQKDTYTMKEVLFYLGQYIMTKRLYDEKQQHIVYCSNDLLGDLFGVPSFSVKEHRKIYTMIYRNLVVVNQQESSDS","proteinLength":"Fragment","predictedMolecularWeight":"17.5 kDa","actualMolecularWeight":null,"aminoAcidEnd":118,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q00987","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

MDM2 also known as murine double minute 2 is an important regulator of the p53 tumor suppressor protein. It functions as an E3 ubiquitin ligase targeting p53 for proteasomal degradation. The MDM2 protein has a molecular weight of approximately 55 kDa. It is expressed in various human tissues with higher levels in rapidly dividing cells. MDM2 interacts through its N-terminal domain with the transactivation domain of p53 inhibiting its transcriptional activity.
Biological function summary

The MDM2 protein plays a central role in cell cycle control and apoptosis regulation. It forms a complex with p53 which modulates p53's stability and activity. By binding to p53 MDM2 prevents p53 from inducing cell cycle arrest or apoptosis in response to DNA damage or oncogenic signals. Its interaction allows cells to proliferate even in the presence of potential growth-arrest signals maintaining homeostasis under normal physiological conditions.

Pathways

MDM2 and p53 form a critical axis within the DNA damage response and tumorigenesis pathways. The p53-MDM2 feedback loop is a well-studied mechanism that balances cell survival and death. When DNA damage occurs p53 gets activated and in turn upregulates MDM2 expression creating a feedback loop. Other proteins like ARF also interact with MDM2 inhibiting its activity towards p53 and thereby enhancing p53 function during cellular stress.

Mutations or overexpression of the MDM2 protein are often associated with various cancers including sarcoma and breast cancer. In these cancers MDM2 amplification leads to enhanced degradation of p53 resulting in unchecked cell proliferation. MDM2's involvement in these pathologies highlights its potential as a therapeutic target with inhibitors like Nutlin-3 being developed to disrupt the MDM2-p53 interaction. The relationship between MDM2 and other proteins such as HDM201 in the context of p53 alterations further highlights its importance in cancer biology.
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Specifications

Form

Liquid

Additional notes

Purity is lot specific. Please contact our technical Support team for details.

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General info

Function

E3 ubiquitin-protein ligase that mediates ubiquitination of p53/TP53, leading to its degradation by the proteasome (PubMed : 29681526). Inhibits p53/TP53- and p73/TP73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Also acts as a ubiquitin ligase E3 toward itself and ARRB1. Permits the nuclear export of p53/TP53. Promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma RB1 protein. Inhibits DAXX-mediated apoptosis by inducing its ubiquitination and degradation. Component of the TRIM28/KAP1-MDM2-p53/TP53 complex involved in stabilizing p53/TP53. Also a component of the TRIM28/KAP1-ERBB4-MDM2 complex which links growth factor and DNA damage response pathways. Mediates ubiquitination and subsequent proteasome degradation of DYRK2 in nucleus. Ubiquitinates IGF1R and SNAI1 and promotes them to proteasomal degradation (PubMed : 12821780, PubMed : 15053880, PubMed : 15195100, PubMed : 15632057, PubMed : 16337594, PubMed : 17290220, PubMed : 19098711, PubMed : 19219073, PubMed : 19837670, PubMed : 19965871, PubMed : 20173098, PubMed : 20385133, PubMed : 20858735, PubMed : 22128911). Ubiquitinates DCX, leading to DCX degradation and reduction of the dendritic spine density of olfactory bulb granule cells (By similarity). Ubiquitinates DLG4, leading to proteasomal degradation of DLG4 which is required for AMPA receptor endocytosis (By similarity). Negatively regulates NDUFS1, leading to decreased mitochondrial respiration, marked oxidative stress, and commitment to the mitochondrial pathway of apoptosis (PubMed : 30879903). Binds NDUFS1 leading to its cytosolic retention rather than mitochondrial localization resulting in decreased supercomplex assembly (interactions between complex I and complex III), decreased complex I activity, ROS production, and apoptosis (PubMed : 30879903).

Sequence similarities

Belongs to the MDM2/MDM4 family.

Post-translational modifications

Phosphorylation on Ser-166 by SGK1 activates ubiquitination of p53/TP53. Phosphorylated at multiple sites near the RING domain by ATM upon DNA damage; this prevents oligomerization and E3 ligase processivity and impedes constitutive p53/TP53 degradation.. Autoubiquitination leads to proteasomal degradation; resulting in p53/TP53 activation it may be regulated by SFN. Also ubiquitinated by TRIM13. Deubiquitinated by USP2 leads to its accumulation and increases deubiquitination and degradation of p53/TP53. Deubiquitinated by USP7 leading to its stabilization.

Subcellular localisation

Nucleus

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Product protocols

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Target data

E3 ubiquitin-protein ligase that mediates ubiquitination of p53/TP53, leading to its degradation by the proteasome (PubMed : 29681526). Inhibits p53/TP53- and p73/TP73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Also acts as a ubiquitin ligase E3 toward itself and ARRB1. Permits the nuclear export of p53/TP53. Promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma RB1 protein. Inhibits DAXX-mediated apoptosis by inducing its ubiquitination and degradation. Component of the TRIM28/KAP1-MDM2-p53/TP53 complex involved in stabilizing p53/TP53. Also a component of the TRIM28/KAP1-ERBB4-MDM2 complex which links growth factor and DNA damage response pathways. Mediates ubiquitination and subsequent proteasome degradation of DYRK2 in nucleus. Ubiquitinates IGF1R and SNAI1 and promotes them to proteasomal degradation (PubMed : 12821780, PubMed : 15053880, PubMed : 15195100, PubMed : 15632057, PubMed : 16337594, PubMed : 17290220, PubMed : 19098711, PubMed : 19219073, PubMed : 19837670, PubMed : 19965871, PubMed : 20173098, PubMed : 20385133, PubMed : 20858735, PubMed : 22128911). Ubiquitinates DCX, leading to DCX degradation and reduction of the dendritic spine density of olfactory bulb granule cells (By similarity). Ubiquitinates DLG4, leading to proteasomal degradation of DLG4 which is required for AMPA receptor endocytosis (By similarity). Negatively regulates NDUFS1, leading to decreased mitochondrial respiration, marked oxidative stress, and commitment to the mitochondrial pathway of apoptosis (PubMed : 30879903). Binds NDUFS1 leading to its cytosolic retention rather than mitochondrial localization resulting in decreased supercomplex assembly (interactions between complex I and complex III), decreased complex I activity, ROS production, and apoptosis (PubMed : 30879903).
See full target information MDM2
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Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Biopolymers 106:853-863 PubMed27287767

2016

Development of cell-penetrating peptide-based drug leads to inhibit MDMX:p53 and MDM2:p53 interactions.

Applications

Unspecified application

Species

Unspecified reactive species

Grégoire Philippe,Yen-Hua Huang,Olivier Cheneval,Nicole Lawrence,Zhen Zhang,David P Fairlie,David J Craik,Aline Dantas de Araujo,Sónia Troeira Henriques
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