Murine Double Minute2 (MDM2)

Specification

• Cat#: THP-0260
• Product Name: Murine Double Minute2 (MDM2)
• Description: Murine Double Minute2 (MDM2) is E. coli-derived human MDM2/HDM2 protein.
• Species: Human
• Molecular Weight: 55 kDa
• Source: E. coli
• Introduction: Double minute 2 protein (Mdm2, also known as Hdm2) is a RING-finger Ubiquitin E3 ligase that acts as a major regulator of the tumor suppressor p53. Mdm2 inhibits p53-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. The E3 ligase activity is confined to the C-terminal domain of Mdm2 and is responsible for the ubiquitinylation and subsequent proteasomal degradation of p53. Although the isolated RING domain is capable of p53 ubiquitinylation, other regions of the protein including a central acidic domain are also crucial for full E3 ligase activity. Mdm2 also regulates its own intracellular levels by auto-ubiquitinylation, and can be SUMOylated which decreases autoubiquitinylation activity but increases activity toward p53. Mdm2 also affects the cell cycle and apoptosis through interactions with other proteins such as retinoblastoma1 (pRB) and ribosomal protein L5. This recombinant protein is untagged.
• Purity: >85%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain.
• Biological Activity: Recombinant Human Mdm2/Hdm2 is a RING finger Ubiquitin ligase (E3) that functions downstream of a Ubiquitin-activating (E1) enzyme and a Ubiquitin-conjugating (E2) enzyme to conjugate Ubiquitin to substrate proteins. Reaction conditions will need to be optimized for each specific application. We recommend an initial Recombinant Human Mdm2/Hdm2 concentration of 0.5-5 μM.
• Application: The E3 ligase activity is confined to the C-terminal domain of Mdm2 and is responsible for the ubiquitinylation and subsequent proteasomal degradation of p53, and can be SUMOylated which decreases autoubiquitinylation activity but increases activity toward p53.