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Mouse Anti-MDM2 Recombinant Antibody (1A7) (CBMAB-A5362-LY)

The product is antibody recognizes MDM2. The antibody 1A7 immunoassay techniques such as: WB, ELISA.
See all MDM2 antibodies
Published Data
Fig.1 Representative western blot showing induction of p21, p53 and MDM2.
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Summary

Host Animal
Mouse
Specificity
Human
Clone
1A7
Antibody Isotype
IgG1, κ
Application
WB, ELISA

Basic Information

Immunogen
MDM2 (NP_002383, 101 a.a. ~ 200 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.
Specificity
Human
Antibody Isotype
IgG1, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Purity
> 95% Purity determined by SDS-PAGE.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
MDM2 Proto-Oncogene
Introduction
This gene is a target gene of the transcription factor tumor protein p53. The encoded protein is a nuclear phosphoprotein that binds and inhibits transactivation by tumor protein p53, as part of an autoregulatory negative feedback loop. Overexpression of this gene can result in excessive inactivation of tumor protein p53, diminishing its tumor suppressor function. This protein has E3 ubiquitin ligase activity, which targets tumor protein p53 for proteasomal degradation. This protein also affects the cell cycle, apoptosis, and tumorigenesis through interactions with other proteins, including retinoblastoma 1 and ribosomal protein L5. More than 40 different alternatively spliced transcript variants have been isolated from both tumor and normal tissues. [provided by RefSeq]
Entrez Gene ID
4193
UniProt ID
Q00987
Alternative Names
HDMX; MGC71221; hdm2
Function
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).
Biological Process
Amyloid fibril formation Source: CAFA
Apoptotic process Source: UniProtKB
Atrial septum development Source: Ensembl
Atrioventricular valve morphogenesis Source: Ensembl
Blood vessel development Source: Ensembl
Blood vessel remodeling Source: Ensembl
Cardiac septum morphogenesis Source: Ensembl
Cellular response to actinomycin D Source: CAFA
Cellular response to gamma radiation Source: CAFA
Cellular response to hypoxia Source: UniProtKB
DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: UniProtKB
Endocardial cushion morphogenesis Source: Ensembl
Establishment of protein localization Source: BHF-UCL
Negative regulation of DNA damage response, signal transduction by p53 class mediator Source: BHF-UCL
Negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator Source: CAFA
Negative regulation of signal transduction by p53 class mediator Source: UniProtKB
Negative regulation of transcription, DNA-templated Source: UniProtKB
Negative regulation of transcription by RNA polymerase II Source: UniProtKB
Positive regulation of cell population proliferation Source: BHF-UCL
Positive regulation of mitotic cell cycle Source: UniProtKB
Positive regulation of muscle cell differentiation Source: Ensembl
Positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: BHF-UCL
Proteasome-mediated ubiquitin-dependent protein catabolic process Source: ARUK-UCL
Protein autoubiquitination Source: UniProtKB
Protein-containing complex assembly Source: UniProtKB
Protein destabilization Source: BHF-UCL
Protein localization to nucleus Source: BHF-UCL
Protein polyubiquitination Source: ARUK-UCL
Protein ubiquitination Source: UniProtKB
Proteolysis involved in cellular protein catabolic process Source: CAFA
Regulation of cell cycle Source: BHF-UCL
Regulation of heart rate Source: Ensembl
Regulation of protein catabolic process Source: UniProtKB
Regulation of transcription by RNA polymerase II Source: GO_Central
Response to antibiotic Source: UniProtKB
Transcription factor catabolic process Source: ParkinsonsUK-UCL
Traversing start control point of mitotic cell cycle Source: Ensembl
Ubiquitin-dependent protein catabolic process Source: UniProtKB
Ventricular septum development Source: Ensembl
Cellular Location
Nucleus
nucleoplasm
nucleolus
Nucleus
Cytoplasm
Note: Expressed predominantly in the nucleoplasm. Interaction with ARF(P14) results in the localization of both proteins to the nucleolus. The nucleolar localization signals in both ARF(P14) and MDM2 may be necessary to allow efficient nucleolar localization of both proteins. Colocalizes with RASSF1 isoform A in the nucleus.
Involvement in disease
Seems to be amplified in certain tumors (including soft tissue sarcomas, osteosarcomas and gliomas). A higher frequency of splice variants lacking p53 binding domain sequences was found in late-stage and high-grade ovarian and bladder carcinomas. Four of the splice variants show loss of p53 binding.
Lessel-Kubisch syndrome (LSKB):
An autosomal recessive progeroid syndrome characterized by short stature, pinched facial features, prematurely gray hair, scleroderma-like skin changes, small kidneys and consecutive kidney failure, followed by severe arterial hypertension.
PTM
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.

Mukherjee, N., Bhunia, D., Garai, P. K., Mondal, P., Barman, S., & Ghosh, S. (2024). Designed novel nuclear localizing anticancer peptide targets p53 negative regulator MDM2 protein. Journal of Peptide Science, 30(1), e3535.

Zhu, H., Gao, H., Ji, Y., Zhou, Q., Du, Z., Tian, L., ... & Zhou, Z. (2022). Targeting p53–MDM2 interaction by small-molecule inhibitors: Learning from MDM2 inhibitors in clinical trials. Journal of Hematology & Oncology, 15(1), 91.

Blondel-Tepaz, E., Leverve, M., Sokrat, B., Paradis, J. S., Kosic, M., Saha, K., ... & Scott, M. G. (2021). The RanBP2/RanGAP1-SUMO complex gates β-arrestin2 nuclear entry to regulate the Mdm2-p53 signaling axis. Oncogene, 40(12), 2243-2257.

Klein, A. M., de Queiroz, R. M., Venkatesh, D., & Prives, C. (2021). The roles and regulation of MDM2 and MDMX: it is not just about p53. Genes & Development, 35(9-10), 575-601.

Chibaya, L., Karim, B., Zhang, H., & Jones, S. N. (2021). Mdm2 phosphorylation by Akt regulates the p53 response to oxidative stress to promote cell proliferation and tumorigenesis. Proceedings of the National Academy of Sciences, 118(4), e2003193118.

Zhang, X., Min, X., Wang, S., Sun, N., & Kim, K. M. (2020). Mdm2-mediated ubiquitination of β-arrestin2 in the nucleus occurs in a Gβγ-and clathrin-dependent manner. Biochemical Pharmacology, 178, 114049.

Konopleva, M., Martinelli, G., Daver, N., Papayannidis, C., Wei, A., Higgins, B., ... & Andreeff, M. (2020). MDM2 inhibition: an important step forward in cancer therapy. Leukemia, 34(11), 2858-2874.

Wang, W., Qin, J. J., Rajaei, M., Li, X., Yu, X., Hunt, C., & Zhang, R. (2020). Targeting MDM2 for novel molecular therapy: Beyond oncology. Medicinal research reviews, 40(3), 856-880.

Hou, H., Sun, D., & Zhang, X. (2019). The role of MDM2 amplification and overexpression in therapeutic resistance of malignant tumors. Cancer cell international, 19(1), 216.

Choi, Y. M., An, S., Bae, S., & Jung, J. H. (2019). Mdm2 is required for HDAC3 monoubiquitination and stability. Biochemical and Biophysical Research Communications, 517(2), 353-358.

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For research use only. Not intended for any clinical use.

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