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Phospho-MDM2 (Thr218) Polyclonal Antibody, RBITC Conjugated

Product Specifications

Background

E3 ubiquitin-protein ligase that mediates ubiquitination of p53/TP53, leading to its degradation by the proteasome. Inhibits p53/TP53- and p73/TP73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Also acts as a ubiquitin ligase E3 toward itself and ARRB1. Permits the nuclear export of p53/TP53. Promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma RB1 protein. Inhibits DAXX-mediated apoptosis by inducing its ubiquitination and degradation. Component of the TRIM28/KAP1-MDM2-p53/TP53 complex involved in stabilizing p53/TP53. Also component of the TRIM28/KAP1-ERBB4-MDM2 complex which links growth factor and DNA damage response pathways. Mediates ubiquitination and subsequent proteasome degradation of DYRK2 in nucleus. Ubiquitinates IGF1R and SNAI1 and promotes them to proteasomal degradation.

Synonyms

HDMX; hdm2; ACTFS; E3 ubiquitin-protein ligase Mdm2; Double minute 2 protein; Oncoprotein Mdm2; p53-binding protein Mdm2; MDM2

Gene ID

4193

Swiss Prot

Q00987

Modification Site

Thr218

Cellular Locus

Cytoplasm, Nucleus

Host

Rabbit

Cross Reactivity

Human, Mouse, Rat

Target

Phospho-MDM2 (Thr218)

Clonality

Polyclonal

Isotype

IgG

Conjugation

RBITC

Source

KLH conjugated synthetic phosphopeptide derived from human MDM2 around the phosphorylation site of Thr218

Applications

WB, FCM, IF (IHC-P), IF (IHC-F), IF (ICC)

Purification

Purified by Protein A.

Excitation Emission

570nm/595nm

Concentration

1µg/µl

Dilution

WB (1:300-5000), FCM (1:20-100), IF (IHC-P) (1:50-200), IF (IHC-F) (1:50-200), IF (ICC) (1:50-200)

Buffer

Aqueous buffered solution containing 0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.

Modification

Phosphorylation

Storage Conditions

Store at -20°C. Aliquot into multiple vials to avoid repeated freeze-thaw cycles.

Gene ID URL

4193

Predicted Cross Reactivity

Dog, Cow, Horse

Curated Selection

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