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OP115

Sigma-Aldrich

Anti-MDM2 (Ab-2) Mouse mAb (2A10)

liquid, clone 2A10, Calbiochem®

Synonym(s):

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

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

Quality Level

100

antibody form

purified antibody

antibody product type

primary antibodies

clone

2A10, monoclonal

form

liquid

contains

≤0.1% sodium azide as preservative

species reactivity

human

manufacturer/tradename

Calbiochem®

storage condition

do not freeze

isotype

IgG2a

shipped in

wet ice

storage temp.

2-8°C

target post-translational modification

unmodified

Gene Information

human ... MDM2(4193)

General description

Purified mouse monoclonal antibody (see application references). Recognizes the ~90 kDa (apparent MW) MDM2 protein.
Recognizes the ~90 kDa (apparent MW) MDM2 protein in A549 cells.
This Anti-MDM2 (Ab-2) Mouse mAb (2A10) is validated for use in Immunoblotting, Immunofluorescence, Immunoprecipitation, Paraffin Sections for the detection of MDM2 (Ab-2).

Immunogen

Epitope: within amino acids 294-339
Human
human MDM2 protein

Application


Immunoblotting (2 g/ml)
Immunofluorescence (1 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, 0.2% gelatin, pH 7.5.

Analysis Note

Positive Control
A549 cells or most tissues

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.
Chen, J., et al. 1993. Mol. Cell Biol.13, 4107.
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 Code

12 - Non Combustible Liquids

WGK

nwg

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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Kwong-Him To et al.
BMC cancer, 12, 69-69 (2012-02-18)
Most human cancers show inactivation of both pRB- and p53-pathways. While retinoblastomas are initiated by loss of the RB1 tumor suppressor gene, TP53 mutations have not been found. High expression of the p53-antagonist MDM2 in human retinoblastomas may compromise p53
Tomohiro Matsumoto et al.
The journal of physiological sciences : JPS, 69(2), 317-326 (2018-11-28)
The purpose of the present study was to determine the effects of transcutaneous CO2 application on the blood flow and capillary architecture of the soleus muscle in rats with streptozotocin (STZ)-induced hyperglycemia. Wistar rats were randomly divided into four groups:
Thomas J Huot et al.
Molecular and cellular biology, 22(23), 8135-8143 (2002-11-06)
The INK4a/ARF tumor suppressor locus is implicated in the senescence-like growth arrest provoked by oncogenic Ras in primary cells. INK4a and ARF are distinct proteins encoded by transcripts in which a shared exon is decoded in alternative reading frames. Here
Liang Zhao et al.
Cancer research, 69(24), 9439-9447 (2009-11-26)
Src family tyrosine kinases (SFK) regulate cell proliferation, and increased SFK activity is common in human carcinomas, including cutaneous squamous cell carcinomas (SCC) and its precursors. The elevated SFK activity in cutaneous SCCs was modeled using K14-Fyn Y528F transgenic mice
Nadezhda Tikhmyanova et al.
PLoS pathogens, 13(7), e1006517-e1006517 (2017-07-18)
The chemical probe C60 efficiently triggers Epstein-Barr Virus (EBV) reactivation from latency through an unknown mechanism. Here, we identify the Cullin exchange factor CAND1 as a biochemical target of C60. We also identified CAND1 in an shRNA library screen for
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