OP145
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
Productos recomendados
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
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.
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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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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