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Sigma-Aldrich

Anti-MDM2 (Ab-5) Mouse mAb (4B2C1.11)

liquid, clone 4B2C1.11, Calbiochem®

Sinonimo/i:

Anti-Ubiquitin Protein Ligase, Anti-p53 Binding Protein, Ant-Murine Double Minute Chromosome-2

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About This Item

Codice UNSPSC:
12352203
NACRES:
NA.43

Origine biologica

mouse

Livello qualitativo

Forma dell’anticorpo

purified antibody

Tipo di anticorpo

primary antibodies

Clone

4B2C1.11, monoclonal

Forma fisica

liquid

non contiene

preservative

Reattività contro le specie

human

Produttore/marchio commerciale

Calbiochem®

Condizioni di stoccaggio

OK to freeze
avoid repeated freeze/thaw cycles

Isotipo

IgG1

Condizioni di spedizione

wet ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

human ... MDM2(4193)

Descrizione generale

Purified mouse monoclonal antibody. Recognizes the ~90 kDa (apparent MW) MDM2 protein.
Recognizes the ~90 kDa (apparent MW) MDM2 protein in A549 and MCF-7 cells and breast carcinoma tissue.
This Anti-MDM2 (Ab-5) Mouse mAb (4B2C1.11) is validated for use in Immunoblotting, Immunofluorescence, Immunoprecipitation, Paraffin Sections for the detection of MDM2 (Ab-5).

Immunogeno

Human
recombinant, human MDM2

Applicazioni


Immunoblotting (2 g/ml, chemiluminescence)
Immunofluorescence (2.5 g/ml)
Immunoprecipitation (1 g/reaction, see application references)
Paraffin Sections (2.5 g/ml, heat pre-treatment required)

Confezionamento

Please refer to vial label for lot-specific concentration.

Attenzione

Toxicity: Standard Handling (A)

Stato fisico

In 50 mM sodium phosphate buffer, 50% glycerol, pH 7.5.

Ricostituzione

Following initial thaw, aliquot and freeze (-20°C).

Risultati analitici

Positive Control
A549 or MCF7 cells or breast carcinoma tissue

Altre note

Antibody should be titrated for optimal results in individual systems.
Marchetti, A., et al. 1995. J. Pathol.175, 31.
Barak, Y., et al. 1993. EMBO. J.12, 461.
Ladanyi, M., et al. 1993. Cancer Res.53, 16.
Leach, F.S., et al. 1993. Cancer Res.53, 2231.
Oliner, J.D., et al. 1993. Nature362, 857.
Momand, J., et al. 1992. Cell69, 1237.
Oliner, J.D., et al. 1992. Nature358, 80.
Fakharzadeh, S.S., et al. 1991. EMBO J.10, 1565.

Note legali

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

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Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

WGK 3


Certificati d'analisi (COA)

Cerca il Certificati d'analisi (COA) digitando il numero di lotto/batch corrispondente. I numeri di lotto o di batch sono stampati sull'etichetta dei prodotti dopo la parola ‘Lotto’ o ‘Batch’.

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Paula M Hauck et al.
Molecular cancer research : MCR, 15(11), 1598-1607 (2017-08-09)
Metastasis of cancer cells to distant organ systems is a complex process that is initiated with the programming of cells in the primary tumor. The formation of distant metastatic foci is correlated with poor prognosis and limited effective treatment options.
Xiongbin Lu et al.
Cancer cell, 12(4), 342-354 (2007-10-16)
The tumor suppressor p53 is a transcription factor that responds to cellular stresses by initiating cell cycle arrest or apoptosis. One transcriptional target of p53 is Mdm2, an E3 ubiquitin ligase that interacts with p53 to promote its proteasomal degradation
Daniel Garcia et al.
Genes & development, 25(16), 1746-1757 (2011-08-20)
MdmX, also known as Mdm4, is a critical negative regulator of p53, and its overexpression serves to block p53 tumor suppressor function in many cancers. Consequently, inhibiting MdmX has emerged as an attractive approach to restoring p53 function in those
A Carpentieri et al.
Cell death & disease, 6, e1974-e1974 (2015-11-13)
Current hypothesis suggest that tumors can originate from adult cells after a process of 'reprogramming' driven by genetic and epigenetic alterations. These cancer cells, called cancer stem cells (CSCs), are responsible for the tumor growth and metastases. To date, the
Weijia Cai et al.
Nature communications, 10(1), 5800-5800 (2019-12-22)
p53 acetylation is indispensable for its transcriptional activity and tumor suppressive function. However, the identity of reader protein(s) for p53 acetylation remains elusive. PBRM1, the second most highly mutated tumor suppressor gene in kidney cancer, encodes PBRM1. Here, we identify

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