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Recombinant Human MDM2/HDM2 Protein, CF Summary
Additional Information
Details of Functionality
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.
Source
E. coli-derived human MDM2/HDM2 protein Met1 - Pro491
>85%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
55 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Publications
Read Publications using E3-204 in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
6 months from date of receipt, -70 °C as supplied.
3 months, -70 °C under sterile conditions after opening.
Buffer
Supplied as a solution in HEPES, NaCl, TCEP and Glycerol.
Purity
>85%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human MDM2/HDM2 Protein, CF
ACTFS
HDM2
HDMX
MDM2 oncogene, E3 ubiquitin protein ligase
MDM2
Background
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.
Brooks C.L., et al. (2007) J.Biol.Chem 282:22804.
Bushmann T., et al. (2001) J.Biol.Chem 276:40389.
Dornan D, et al. (2004) Nature 429:86.
Grossman S.R., et al. (2003) Science 300:342.
Hu M., et al. (2006) PLoS Biol. 4:228.
Kawai H., et al. (2003) Mol. Cell. Biol. 23:4939.
Lai Z., et al. (2001) J.Biol.Chem 276:31357.
Li M, et al. (2003) Science 301:1972.
Linares L.K., et al. (2003) Proc.Natl.Acad.Sci. 100:12009.
Sheng Y, et al. (2006) Nat.Struc.Mol.Biol. 13:285.
Wu H., et al. (2011) Nature Med. 17:347.
Yan Y. and Chen J. (2005) Biochem. Biophys. Res. Comm. 332:702.
Yu G.W., et al. (2006) Proc.Natl.Acad.Sci. 103:1227.
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