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M7815

Sigma-Aldrich

Anti-MDM2 antibody ,Mouse monoclonal

clone HDM2-323, purified from hybridoma cell culture

Synonym(s):

Anti-ACTFS, Anti-HDMX, Anti-LSKB, Anti-hdm2

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

conjugate

unconjugated

antibody form

purified from hybridoma cell culture

antibody product type

primary antibodies

clone

HDM2-323, monoclonal

form

buffered aqueous solution

mol wt

antigen ~90 kDa

species reactivity

human, mouse

concentration

~2 mg/mL

technique(s)

indirect ELISA: suitable
microarray: suitable
western blot: 1-2 μg/mL (whole cell extract of 293T cells transfected with human MDM2)

isotype

IgG2a

UniProt accession no.

Q00987

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... MDM2(4193)
mouse ... Mdm2(17246)

General description

Monoclonal Anti-MDM2 (mouse IgG2a isotype) is derived from the HDM2-323 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice. MDM2 (the human homologue of Mdm2, a 90 kDa molecule), is a transcriptional target of p53.

Immunogen

synthetic peptide corresponding to amino acids 389-402 of human MDM2 conjugated to KLH.

Application

Anti-MDM2 antibody, Mouse monoclonal has been used in western blotting and enzyme linked immunosorbent assay (ELISA).

Biochem/physiol Actions

MDM2 functions in the activation of p53 resulting in MDM2 expression, which consequently inhibits p53 transcriptional function. MDM2 accomplishes this inhibition in two ways: because of its physical interaction with p53, MDM2 both represses p53 transcriptional activity and mediates the degradation of p53. Overexpression of MDM2 results in reduced quantities of coexpressed p53, and disruption of the p53-MDM2 interaction by mutation results in both activation and accumulation of p53. MDM2 protein has been shown to activate cell proliferation by stimulating the S-phase-inducing transcription factors, E2F1/DP1.5 The amplification of the MDM2 gene has been demonstrated in various human neoplasms.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Disclaimer

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.

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Storage Class Code

10 - Combustible liquids

WGK

WGK 3

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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Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53
Fang S, et al.
The Journal of Biological Chemistry, 275(12), 8945-8951 (2000)
Dan Zhu et al.
The Journal of clinical investigation, 125(4), 1497-1508 (2015-03-10)
Synaptic plasticity is the ability of synapses to modulate the strength of neuronal connections; however, the molecular factors that regulate this feature are incompletely understood. Here, we demonstrated that mice lacking brain-specific angiogenesis inhibitor 1 (BAI1) have severe deficits in
Zehavit Goldberg et al.
The EMBO journal, 21(14), 3715-3727 (2002-07-12)
The p53 tumor suppressor is inhibited and destabilized by Mdm2. However, under stress conditions, this downregulation is relieved, allowing the accumulation of biologically active p53. Recently we showed that c-Abl is important for p53 activation under stress conditions. In response
Xiaobin Wu et al.
OncoTargets and therapy, 11, 3111-3117 (2018-06-07)
The role of dysfunction of MCPH1, a recently identified tumor suppressor gene, has not yet been established in lung cancer. In our previous study, it was reported that MCPH1 expression is downregulated in lung cancer tissues and that MCPH1 overexpression
Shuichi Fujioka et al.
The Journal of biological chemistry, 279(26), 27549-27559 (2004-04-23)
Both pro- and antiapoptotic activities of NF-kappaB transcription factor have been observed; however, less is known about the mechanism by which NF-kappaB induces apoptosis. To elucidate how NF-kappaB regulates proapoptotic signaling, we performed functional analyses using wild-type, ikk1(-/-), ikk2(-/-), rela(-/-)
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