protein

MDM2 Protein, Human

HY-P701593

5 μg;10 μg;20 μg;50 μg;100 μg

128;205;310;580;930 USD

MDM2 Protein, Human

proteins

E. coli

5 μg;10 μg;20 μg;50 μg;100 μg

128;205;310;580;930 USD

MDM2 protein is a key E3 ubiquitin protein ligase that coordinates cellular processes by ubiquitinating and degrading p53/TP53 and inhibiting its tumor suppressor function. In addition to p53/TP53 regulation, MDM2 inhibits p53/TP53- and p73/TP73-mediated responses, self-ubiquitinates, and targets ARRB1 for degradation. MDM2 Protein, Human is the recombinant human-derived MDM2 protein, expressed by E. coli , with tag free. The total length of MDM2 Protein, Human is 95 a.a., with molecular weight of 11.1 kDa.

Human

MDM2 Protein, an E3 ubiquitin-protein ligase, plays a central role in the intricate regulation of cellular processes by mediating the ubiquitination and subsequent proteasomal degradation of the tumor suppressor p53/TP53, leading to its downregulation. Beyond its interaction with p53/TP53, MDM2 inhibits p53/TP53- and p73/TP73-mediated cell cycle arrest and apoptosis by binding to their transcriptional activation domain, highlighting its role as a negative regulator of these critical cellular responses. Not limited to its interactions with p53/TP53, MDM2 functions as a ubiquitin ligase E3 toward itself and ARRB1, permitting the nuclear export of p53/TP53 and promoting the proteasome-dependent ubiquitin-independent degradation of retinoblastoma RB1 protein. Additionally, MDM2 inhibits DAXX-mediated apoptosis by inducing its ubiquitination and degradation, demonstrating its versatile involvement in apoptotic pathways. As a component of various complexes, including TRIM28/KAP1-MDM2-p53/TP53 and TRIM28/KAP1-ERBB4-MDM2, MDM2 links growth factor and DNA damage response pathways. It further mediates ubiquitination and proteasome degradation of DYRK2, IGF1R, SNAI1, DCX, and DLG4, influencing diverse cellular functions such as dendritic spine density, receptor endocytosis, and mitochondrial respiration. Through its interactions with NDUFS1, MDM2 negatively regulates mitochondrial respiration, leading to increased oxidative stress and commitment to the mitochondrial pathway of apoptosis. These multifaceted roles underscore the intricate regulatory functions of MDM2 in cellular homeostasis and stress responses.

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

Greater than 90% as determined by reducing SDS-PAGE.

Supplied as a 0.22 μm filtered solution of 50 mM Tris-HCl, pH 7.5, 200 mM NaCl, 20% glycerol, 1mM DTT.

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