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Key Documents

OP145

Sigma-Aldrich

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

liquid, clone 4B2C1.11, Calbiochem®

Sinónimos:

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

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.43

biological source

mouse

Quality Level

antibody form

purified antibody

antibody product type

primary antibodies

clone

4B2C1.11, monoclonal

form

liquid

does not contain

preservative

species reactivity

human

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze
avoid repeated freeze/thaw cycles

isotype

IgG1

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... MDM2(4193)

General description

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).

Immunogen

Human
recombinant, human MDM2

Application


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)

Packaging

Please refer to vial label for lot-specific concentration.

Warning

Toxicity: Standard Handling (A)

Physical form

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

Reconstitution

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

Analysis Note

Positive Control
A549 or MCF7 cells or breast carcinoma tissue

Other Notes

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.

Legal Information

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

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Storage Class

10 - Combustible liquids

wgk_germany

WGK 3


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Visite la Librería de documentos

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.
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
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

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