Rabbit Polyclonal MDM2 phospho S185 antibody. Suitable for WB and reacts with Human samples. Cited in 2 publications.
IgG
Rabbit
Preservative: 0.01% Sodium azide
Constituents: 0.88% Sodium chloride, 0.424% Tripotassium orthophosphate
Liquid
Polyclonal
WB | |
---|---|
Human | Tested |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info 1/500 - 1/2000 | Notes - |
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E3 ubiquitin-protein ligase that mediates ubiquitination of p53/TP53, leading to its degradation by the proteasome. 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 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).
E3 ubiquitin-protein ligase Mdm2, Double minute 2 protein, Oncoprotein Mdm2, RING-type E3 ubiquitin transferase Mdm2, p53-binding protein Mdm2, Hdm2, MDM2
Rabbit Polyclonal MDM2 phospho S185 antibody. Suitable for WB and reacts with Human samples. Cited in 2 publications.
E3 ubiquitin-protein ligase Mdm2, Double minute 2 protein, Oncoprotein Mdm2, RING-type E3 ubiquitin transferase Mdm2, p53-binding protein Mdm2, Hdm2, MDM2
IgG
Rabbit
Preservative: 0.01% Sodium azide
Constituents: 0.88% Sodium chloride, 0.424% Tripotassium orthophosphate
Liquid
Polyclonal
Affinity purification Immunogen
This affinity-purified antibody is directed against the phosphorylated form of mouse MDM2 protein at the pS185 residue. Reactivity occurs against Mouse MDM2 pS185 protein and the antibody is specific for the phosphorylated form of the protein. Reactivity with non-phosphorylated mouse MDM2 is minimal by ELISA and western blot. A BLAST analysis was used to suggest minimal cross reactivity with MDM2 homologues from other sources.
This affinity-purified antibody is directed against the phosphorylated form of mouse MDM2 protein at the pS185 residue. The product was affinity purified from monospecific antiserum by immunoaffinity purification. Antiserum was first purified against the phosphorylated form of the immunizing peptide. The resultant affinity purified antibody was then cross-adsorbed against the non-phosphorylated form of the immunizing peptide.
Blue Ice
-20°C
Upon delivery aliquot
Avoid freeze / thaw cycle
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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.
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.
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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Rabbit polyclonal to phospho MDM 2 (Ser 185) at 1/1000 on 293T cell extract shows a band at 102 kD.
Cells were serum starved for 24 hours:
Lane 1 : control
Lane 2 : treated with IGF-1 (100 ng/ml) for 20 min
All lanes: Western blot - Anti-MDM2 (phospho S185) antibody (ab1094)
Predicted band size: 55 kDa
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