- 文献引用 : 5
|Application ||WB, IHC-P, E|
|Other Names||E3 ubiquitin-protein ligase Mdm2, 632-, Double minute 2 protein, Hdm2, Oncoprotein Mdm2, p53-binding protein Mdm2, MDM2|
|Target/Specificity||This Mdm2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 393-424 amino acids from the C-terminal region of human Mdm2.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein G column, eluted with high and low pH buffers and neutralized immediately, followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Mdm2 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||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.|
|Cellular Location||Nucleus, nucleoplasm. Cytoplasm. Nucleus, nucleolus. Note=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|
|Tissue Location||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|
Author : Zhou G1,2,Duan Y1,2,Ma G1,3,Wu W1,Hu Z1,Chen N1,Chee Y4,Cui J5,Samad A6,Matsubara JA5,Mukai S4,D'Amore PA1,Lei H1.
Invest Ophthalmol Vis Sci. 2017 Oct 1;58(12):5361-5367. doi: 10.1167/iovs.17-22045.
Author : Duan Y1, Ma G2, Huang X2, D\'Amore PA3, Zhang F4, Lei H5.
J Biol Chem. 2016 Jul 29;291(31):16339-47. doi: 10.1074/jbc.M116.729467. Epub 2016 May 31.
Author : Mokhtarzadeh A1,2,3, Parhiz H2, Hashemi M4, Abnous K2, Ramezani M2,4.
Expert Opin Drug Deliv. 2015 Dec 10. [Epub ahead of print]
Author : Guo J1, Yang Y1,2, Yang Y1, Linghu E1, Zhan Q3, Brock MV4, Herman JG4, Zhang B5, Guo M1.
Oncotarget. 2015 Feb 28;6(6):4202-13.
Author : Stevenson LF, Sparks A, Allende-Vega N, Xirodimas DP, Lane DP, Saville MK.
EMBO J. 2007 Feb 21;26(4):976-86. Epub 2007 Feb 8.
Provided below are standard protocols that you may find useful for product applications.
MDM2 is a target of the transcription factor tumor protein p53. The encoded protein is a nuclear phosphoprotein that binds and inhibits transactivation by tumor protein p53, as part of an autoregulatory negative feedback loop. Overexpression of MDM2 can result in excessive inactivation of tumor protein p53, diminishing its tumor suppressor function. This protein has E3 ubiquitin ligase activity, which targets tumor protein p53 for proteasomal degradation. This protein also affects the cell cycle,apoptosis, and tumorigenesis through interactions with other proteins, including retinoblastoma 1 and ribosomal protein L5.
Burch, L.R., et al., J. Mol. Biol. 337(1):115-128 (2004). Schon, O., et al., J. Mol. Biol. 336(1):197-202 (2004). Mantesso, A., et al., J. Oral Pathol. Med. 33(2):96-101 (2004). Shmueli, A., et al., Mol. Cell 13(1):4-5 (2004). Xia, L., et al., Cancer Res. 64(1):221-228 (2004).