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04-1556 Anti-MDM4 Antibody, clone 7A8

Use Anti-MDM4 Antibody, clone 7A8 (mouse monoclonal antibody) validated in WB to detect MDM4 also known as Double minute 4 protein, MDM4-related protein 1, Mdm2-like p53-binding protein, Mdm4 p53 binding protein homolog (mouse).

Anti-MDM4 Antibody, clone 7A8 MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.
Research Category: Apoptosis & Cancer Research Sub-Category: Transcription Factors, Apoptosis - Additional Gene Symbol: MDM4, HDMX, MDMX, MRP1 UniProt Number: O35618
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04-1556
100 µg  
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Key Spec Table

Species ReactivityKey ApplicationsHostFormatAntibody Type
H, MWBMPurifiedMonoclonal Antibody
Description
Catalogue Number04-1556
DescriptionAnti-MDM4 Antibody, clone 7A8
Alternate Names
  • Double minute 4 protein
  • MDM4-related protein 1
  • Mdm2-like p53-binding protein
  • Mdm4 p53 binding protein homolog (mouse)
  • Mdm4, transformed 3T3 cell double minute 4, p53 binding
    protein
  • Mdm4, transformed 3T3 cell double minute 4, p53 binding protein (mouse)
  • Protein Mdmx
  • double minute 4, human homolog of
  • p53-binding protein
  • mouse double minute 4 homolog
  • mouse double minute 4, human homolog of
  • p53-binding protein
  • p53-binding protein
  • p53-binding protein Mdm4
Background InformationMDM4 (sometimes referred to as MDMX) is a member of the MDM family proteins. It is known to inhibit p53 and p73 mediated cell cycle arrest and apoptosis. MDM4 is amplified or overexpressed in 10-20% of tumors and 65% of retinoblastomas. The full-length protein has significant homology to MDM2 and can also bind to and inhibit p53. In both MDM2 and MDM4, this interaction with p53 occurs via a binding domain located in the N-terminal region of the protein. Other similar domains include the C-terminal RING finger motif. Although these proteins share similar domains, MDM2 and MDM4 are non-redundant p53 inhibitors, since normal levels of either protein does not compensate for the loss of the other. Recent evidence suggests complementary activities for these proteins with MDM4 regulating p53 activity, and MDM2 playing a key role in p53 stability.
References
Product Information
FormatPurified
Control
  • HeLa cell lysate
PresentationPurified mouse monoclonal IgG2bκ in buffer containing 0.1 M Tris-Glycine (pH 7.4, 150 mM NaCl) with 0.05% sodium azide.
Quality LevelMQ100
Applications
ApplicationUse Anti-MDM4 Antibody, clone 7A8 (mouse monoclonal antibody) validated in WB to detect MDM4 also known as Double minute 4 protein, MDM4-related protein 1, Mdm2-like p53-binding protein, Mdm4 p53 binding protein homolog (mouse).
Key Applications
  • Western Blotting
Biological Information
ImmunogenHis-tagged recombinant protein corresponding to mouse MDM4.
EpitopeUnknown
Clone7A8
ConcentrationPlease refer to the Certificate of Analysis for the lot-specific concentration.
HostMouse
SpecificityThis antibody recognizes MDM4.
IsotypeIgG2bκ
Species Reactivity
  • Human
  • Mouse
Antibody TypeMonoclonal Antibody
Entrez Gene Number
Gene Symbol
  • MDM4
  • HDMX
  • MDMX
  • MRP1
Purification MethodProtein G Purified
UniProt Number
UniProt SummaryFUNCTION: Inhibits p53- and p73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Inhibits degradation of MDM2. Can reverse MDM2-targeted degradation of p53 while maintaining suppression of p53 transactivation and apoptotic functions. The short isoform is a more potent inhibitor of p53 activity than the long isoform.

SUBUNIT STRUCTURE: Binds to p53, p73 and MDM2.

SUBCELLULAR LOCATION: Nucleus.

TISSUE SPECIFICITY: In all tissues tested. The short isoform is expressed in a variety of transformed cell lines.

DOMAIN: Region I is sufficient for binding p53 and inhibiting its G1 arrest and apoptosis functions. It also binds p73. Region II contains most of a central acidic region and a putative C4-type zinc finger. The RING finger domain which coordinates two molecules of zinc mediates the heterooligomerization with MDM2.

SEQUENCE SIMILARITIES: Belongs to the MDM2/MDM4 family.

Contains 1 RanBP2-type zinc finger.

Contains 1 RING-type zinc finger.

Contains 1 SWIB domain.
Molecular Weight~ 80/27 kDa Observed. There are multiple forms for MDM4. Up to 7 different variants have been reported. Full legth of MDM4 is ~80kDa. The short form of MDM4 (MDM4-S) migrates at approximately 17 and 27kDa. (R. Rallapalli, G. Strachan, B. Cho, W. Mercer‡, and DJ. Hall, 1999, A Novel MDMX Transcript, THE JOURNAL OF BIOLOGICAL CHEMISTRY, 274(12), 8299–8308)
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Quality AssuranceEvaluated by Western Blot in HeLa cell lysate.

Western Blot Analysis: 0.5 µg/ml of this antibody detected MDM4 in 10 µg of HeLa cell lysate.
Usage Statement
  • Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Storage and Shipping Information
Storage ConditionsStable for 1 year at 2-8°C from date of receipt.
Packaging Information
Material Size100 µg
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Catalogue Number GTIN
04-1556 04053252741784

Documentation

Anti-MDM4 Antibody, clone 7A8 SDS

Title

Safety Data Sheet (SDS) 

Anti-MDM4 Antibody, clone 7A8 Certificates of Analysis

TitleLot Number
Anti-MDM4, clone 7A8 3073298
Anti-MDM4, clone 7A8 - 2373429 2373429
Anti-MDM4, clone 7A8 - 2427493 2427493
Anti-MDM4, clone 7A8 - 2443057 2443057
Anti-MDM4, clone 7A8 - 1981630 1981630
Anti-MDM4, clone 7A8 - 2168278 2168278
Anti-MDM4, clone 7A8 - 2343597 2343597
Anti-MDM4, clone 7A8 - 3209742 3209742
Anti-MDM4, clone 7A8 - 3698146 3698146
Anti-MDM4, clone 7A8 - 3928112 3928112
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Newsletters / Publications

Title
Research Focus - Volume 5 2012