E3 ubiquitin-protein ligase Mdm2 Recombinant Protein | Mdm2 recombinant protein

Recombinant Mouse E3 ubiquitin-protein ligase Mdm2

Cat. Num. AAA964250

• Gene Names: Mdm2; Mdm-2; AA415488; 1700007J15Rik
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: E3 ubiquitin-protein ligase Mdm2; Recombinant Mouse E3 ubiquitin-protein ligase Mdm2; Double minute 2 protein; Oncoprotein Mdm2; p53-binding protein Mdm2; Mdm2 recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 1-489. Full Length
• Sequence: MCNTNMSVSTEGAASTSQIPASEQETLVRPKPLLLKLLKSVGAQNDTYTMKEIIFYIGQYIMTKRLYDEKQQHIVYCSNDLLGDVFGVPSFSVKEHRKIYAMIYRNLVAVSQQDSGTSLSESRRQPEGGSDLKDPLQAPPEEKPSSSDLISRLSTSSRRRSISETEENTDELPGERHRKRRRSLSFDPSLGLCELREMCSGGSSSSSSSSSESTETPSHQDLDDGVSEHSGDCLDQDSVSDQFSVEFEVESLDSEDYSLSDEGHELSDEDDEVYRVTVYQTGESDTDSFEGDPEISLADYWKCTSCNEMNPPLPSHCKRCWTLRENWLPDDKGKDKVEISEKAKLENSAQAEEGLDVPDGKKLTENDAKEPCAEEDSEEKAEQTPLSQESDDYSQPSTSSSIVYSSQESVKELKEETQDKDESVESSFSLNAIEPCVICQGRPKNGCIVHGKTGHLMSCFTCAKKLKKRNKPCPVCRQPIQMIVLTYFN

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for Mdm2 recombinant protein

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 th to proteasomal degradation.

References

Tumorigenic potential associated with enhanced expression of a gene that is amplified in a mouse tumor cell line.Fakharzadeh S.S., Trusko S.P., George D.L.EMBO J. 10:1565-1569(1991) Genomic organization of the mouse double minute 2 gene.Jones S.N., Ansari-Lari M.A., Hancock A.R., Jones W.J., Gibbs R.A., Donehower L.A., Bradley A.Gene 175:209-213(1996) The organization and expression of the mdm2 gene.de Oca Luna R.M., Tabor A.D., Eberspaecher H., Hulboy D.L., Worth L.L., Colman M.S., Finlay C.A., Lozano G.Genomics 33:352-357(1996) Multiple murine double minute gene 2 (MDM2) proteins are induced by ultraviolet light.Saucedo L.J., Myers C.D., Perry M.E.J. Biol. Chem. 274:8161-8168(1999) Cooperative signals governing ARF-mdm2 interaction and nucleolar localization of the complex.Weber J.D., Kuo M.-L., Bothner B., DiGiammarino E.L., Kriwacki R.W., Roussel M.F., Sherr C.J.Mol. Cell. Biol. 20:2517-2528(2000) Rapid ATM-dependent phosphorylation of MDM2 precedes p53 accumulation in response to DNA damage.Khosravi R., Maya R., Gottlieb T., Oren M., Shiloh Y., Shkedy D.Proc. Natl. Acad. Sci. U.S.A. 96:14973-14977(1999) A novel cellular protein (MTBP) binds to MDM2 and induces a G1 arrest that is suppressed by MDM2.Boyd M.T., Vlatkovic N., Haines D.S.J. Biol. Chem. 275:31883-31890(2000) Regulation of receptor fate by ubiquitination of activated beta 2-adrenergic receptor and beta-arrestin.Shenoy S.K., McDonald P.H., Kohout T.A., Lefkowitz R.J.Science 294:1307-1313(2001) PML regulates p53 stability by sequestering Mdm2 to the nucleolus.Bernardi R., Scaglioni P.P., Bergmann S., Horn H.F., Vousden K.H., Pandolfi P.P.Nat. Cell Biol. 6:665-672(2004) A novel nuclear interactor of ARF and MDM2 (NIAM) that maintains chromosomal stability.Tompkins V.S., Hagen J., Frazier A.A., Lushnikova T., Fitzgerald M.P., di Tommaso A.D., Ladeveze V., Domann F.E., Eischen C.M., Quelle D.E.J. Biol. Chem. 282:1322-1333(2007)

NCBI and Uniprot Product Information

• NCBI GI #: 570700841
• NCBI GeneID: 17246
• NCBI Accession #: NP_001275515.1
• NCBI GenBank Nucleotide #: NM_001288586.1
• UniProt Accession #: P23804; Q61040; Q64330; Q91XK7
• Molecular Weight: 56.6 kDa
• NCBI Official Full Name: E3 ubiquitin-protein ligase Mdm2
• NCBI Official Synonym Full Names: transformed mouse 3T3 cell double minute 2
• NCBI Official Symbol: Mdm2
• NCBI Official Synonym Symbols: Mdm-2; AA415488; 1700007J15Rik
• NCBI Protein Information: E3 ubiquitin-protein ligase Mdm2
• UniProt Protein Name: E3 ubiquitin-protein ligase Mdm2
• Protein Family: E3 ubiquitin-protein ligase
• UniProt Gene Name: Mdm2
• UniProt Entry Name: MDM2_MOUSE

Uniprot Description

MDM2: a ubiquitin ligase for p53, plays a central role in regulation of the stability of p53 via Akt-mediated MDM2 phosphorylation. Phosphorylation of MDM2 increases its interaction with p300, providing a platform to allow the assembly of the protein complex necessary for MDM2-mediated ubiquitination and degradation of p53. Phosphorylation of MDM2 also blocks its binding to p19ARF, increasing the degradation of p53. Facilitates the nuclear export of p53 and targets it for proteasome-mediated proteolysis. Eight alternatively spliced isoforms have been reported.

Protein type: Oncoprotein; Nucleolus; Inhibitor; EC 6.3.2.19; Ligase; Ubiquitin ligase; EC 6.3.2.-; Ubiquitin conjugating system

Cellular Component: cytoplasm; cytosol; nuclear body; nucleolus; nucleoplasm; nucleus; plasma membrane; protein complex; synapse

Molecular Function: coenzyme F420-0 gamma-glutamyl ligase activity; coenzyme F420-2 alpha-glutamyl ligase activity; enzyme binding; identical protein binding; ligase activity; metal ion binding; p53 binding; peroxisome proliferator activated receptor binding; protein binding; ribosomal S6-glutamic acid ligase activity; ubiquitin protein ligase binding; ubiquitin-protein ligase activity; UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate-D-alanyl-D-alanine ligase activity; zinc ion binding

Biological Process: blood vessel development; blood vessel remodeling; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; establishment of protein localization; heart development; negative regulation of apoptosis; negative regulation of caspase activity; negative regulation of DNA damage response, signal transduction by p53 class mediator; negative regulation of transcription from RNA polymerase II promoter; negative regulation of transcription, DNA-dependent; peptidyl-lysine modification; positive regulation of cell cycle; positive regulation of mitotic cell cycle; positive regulation of proteasomal ubiquitin-dependent protein catabolic process; positive regulation of protein export from nucleus; protein complex assembly; protein destabilization; protein ubiquitination; protein ubiquitination during ubiquitin-dependent protein catabolic process; regulation of gene expression; regulation of heart rate; regulation of protein catabolic process; traversing start control point of mitotic cell cycle