Anti-MDM2 Antibody Picoband® Fluoro647 Conjugated

Mdm2 is an important negative regulator of the p53 tumor suppressor. It is the name of a gene as well as the protein encoded by that gene. Mdm2 protein functions both as an E3 ubiquity lipase that recognizes the N-terminal trans-activation domain (TAD) of the p53 tumor suppressor and an inhibitor of p53 transcriptional activation. Oliner et al. (1992) used MDM2 clones to localize the human gene to chromosome 12q13-q14 by analysis of human-hamster somatic cell hybrids.

A synthetic peptide corresponding to a sequence at the C-terminus of human MDM2, different from the related mouse sequence by two amino acids, and from the related rat sequence by three amino acids.

Ubiquitous. Isoform Mdm2-A, isoform Mdm2-B, isoform Mdm2-C, isoform Mdm2-D, isoform Mdm2-E, isoform Mdm2-F and isoform Mdm2-G are observed in a range of cancers but absent in normal tissues.

Cancer, Cell Biology, Cell Cycle, Cell Cycle Inhibitors, Epigenetics and Nuclear Signaling, Oncoproteins, Oncoproteins/Suppressors, p53 Pathway, Transcription, Ubiquitin & Ubiquitin Like Modifiers

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. .

1. Uhrinova S, Uhrin D, Powers H, et al (2005) . Structure of free MDM2 N-terminal domain reveals conformational adjustments that accompany p53-binding. J. Mol. Biol. 350 (3) : 587–98.

Nucleus, nucleoplasm. Cytoplasm. Nucleus, nucleolus. 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.