MABE281
Anti-MDM2 Antibody, clone 2A10
clone 2A10, from mouse
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Synonym(s):
E3 ubiquitin-protein ligase Mdm2, Double minute 2 protein, Hdm2, Oncoprotein Mdm2, p53-binding protein Mdm2
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
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biological source
mouse
Quality Level
antibody form
culture supernatant
antibody product type
primary antibodies
clone
2A10, monoclonal
species reactivity
human
technique(s)
immunoprecipitation (IP): suitable
western blot: suitable
isotype
IgG2aκ
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Gene Information
human ... MDM2(4193)
General description
MDM2 is an E3 ubiquitin ligase that is most widely studied for its role in regulating the p53 tumor suppressor. MDM2 antagonizes the transcriptional activity of p53 in two main ways. The N-terminal of MDM2 interacts and disables the transactivation domain of p53. In addition, the C-terminal E3 ligase region of MDM2 can attach monoubiquitin to p53 resulting in the transport of p53 from the nucleus to the cytoplasm, thereby preventing the interaction of p53 with target DNA sequences. In addition, MDM2 may also attach polyubiquitin chains to p53, resulting in the degradation of p53 by the proteosome. MDM2 may produce these effects in cooperation with the Mdmx protein. Overall, MDM2 inhibits the ability of p53 to induce cell cycle arrest or apoptosis, and may contribute to oncogenesis.
Application
Anti-MDM2 Antibody, clone 2A10 is a Mouse Monoclonal Antibody for detection of MDM2 also known as E3 ubiquitin-protein ligase Mdm2 or Hdm2 & has been validated in WB & IP.
Immunoprecipitation Analysis: A representative lot was used by an independent laboratory in human lymphoblastoid cell line (NL553) treated with NCS. (Khosravi, R., et al. (1999). PNAS. 96(26):14973–14977.)
Quality
Evaluated by Western Blot in A-549 cell lysate.
Western Blot Analysis: 0.5 µg/mL of this antibody detected MDM2 on 10 µg of A-549 cell lysate.
Western Blot Analysis: 0.5 µg/mL of this antibody detected MDM2 on 10 µg of A-549 cell lysate.
Target description
~90 kDa observed. The calculated molecular weight is 55 kDa, however MDM2 has been shown as a ~90 kDa band in western blots (Erhardt, P., et al. (1997). The Journal of Biological Chemistry. 272:15049-15052.). Uniprot describes many isoforms between 12-56 kDa, which can be highly phosphorylated and ubiquitinated.
Physical form
Format: Purified
Purified mouse monoclonal IgG2aκ cultured supernatant in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Analysis Note
Control
A-549 cell lysate
A-549 cell lysate
Other Notes
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
recommended
Product No.
Description
Pricing
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Shunbin Xiong et al.
Cancer research, 70(18), 7148-7154 (2010-08-26)
High levels of the critical p53 inhibitor Mdm4 is common in tumors that retain a wild-type p53 allele, suggesting that Mdm4 overexpression is an important mechanism for p53 inactivation during tumorigenesis. To test this hypothesis in vivo, we generated transgenic
Vinod Pant et al.
Genes & development, 27(17), 1857-1867 (2013-08-27)
The p53-Mdm2 feedback loop is perceived to be critical for regulating stress-induced p53 activity and levels. However, this has never been tested in vivo. Using a genetically engineered mouse with mutated p53 response elements in the Mdm2 P2 promoter, we
Oliver Bischof et al.
Molecular cell, 22(6), 783-794 (2006-06-24)
Cellular senescence and apoptosis have evolved to restrain unwarranted proliferation of potentially tumorigenic cells. Here we show that overexpression of the E3 SUMO ligase PIASy in normal human fibroblasts recruits the p53 and Rb tumor suppressor pathways to provoke a
Kyle P Feeley et al.
Cancer research, 77(14), 3823-3833 (2017-06-04)
p53 deletion prevents the embryonic lethality of normal tissues lacking Mdm2, suggesting that cells can survive without Mdm2 if p53 is also absent. Here we report evidence challenging this view, with implications for therapeutically targeting Mdm2. Deletion of Mdm2 in
Andrés Pizzorno et al.
Scientific reports, 8(1), 3746-3746 (2018-03-01)
The interplay between influenza A viruses (IAV) and the p53 pathway has been reported in several studies, highlighting the antiviral contribution of p53. Here, we investigated the impact of IAV on the E3-ubiquitin ligase Mdm2, a major regulator of p53
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