Rabbit Anti-MDM2 Polyclonal Antibody #abs130145

abs130145-50ug

1-2 Weeks

201

abs130145-100ug

1-2 Weeks

301

Description

MDM2 is a crucial regulator of the stability of p53, acting as a ubiquitin ligase for this tumor suppressor protein. Its activity is mediated by Akt-mediated MDM2 phosphorylation, which increases the interaction between MDM2 and p300. This interaction provides a platform for the assembly of the protein complex responsible for MDM2-mediated ubiquitination and subsequent degradation of p53. Additionally, phosphorylation of MDM2 blocks its binding to p19ARF, further promoting the degradation of p53.
Furthermore, MDM2 plays a role in facilitating the nuclear exportation of p53, thereby promoting its targeting for proteasome-mediated proteolysis. Notably, the MDM2 gene expresses eight alternatively spliced isoforms, which may have distinct functions in the regulation of p53 stability and other cellular processes. Consequently, the study of MDM2 isoforms and their effects on p53 may contribute to a better understanding of the intricate regulatory networks that control cell proliferation, survival, and death.

Other names

MDM2, also known as HDM2 or HDMX, is an important protein involved in regulating cell growth and division. It functions as an E3 ubiquitin-protein ligase, which means it helps target other proteins for degradation by attaching ubiquitin molecules to them. MDM2 is often referred to as the MDM2 oncogene E3 ubiquitin protein ligase and is considered a key player in tumor development and progression.
In mice, MDM2 is known to bind to the p53 protein, a well-known tumor suppressor. This binding inhibits the activity of p53, preventing it from carrying out its tumor-suppressing functions. Additionally, MDM2 is also observed to bind to a protein called 104kDa, which is found in transformed 3T3 cells. This interaction further enhances MDM2's influence on cell growth and proliferation.
In humans, the MDM2 gene is designated as MDM2_HUMAN and is associated with various cellular processes, including DNA repair, cell cycle regulation, and apoptosis. Its overexpression is frequently observed in many types of cancers and is often linked to poor prognosis and resistance to cancer therapies.
Overall, MDM2 plays a crucial role in modulating the activity of important tumor suppressor proteins like p53, making it an attractive target for therapeutic interventions in cancer treatment.

Source

Rabbit

Specificity

The MDM2 antibody is capable of identifying the total MDM2 present in the body at its natural levels. As a result, it is able to specifically detect the endogenous MDM2 protein.

Species Reactivity

Human;Mouse;Rat;Monkey

Application

Western Blotting (WB) is commonly performed using primary antibody dilutions ranging from 1:500 to 1:3000. Immunohistochemistry (IHC) involves the use of primary antibody dilutions typically ranging from 1:50 to 1:200. For Immunofluorescence (IF) or Immunocytochemistry (ICC), primary antibody dilutions usually vary from 1:100 to 1:500. In Enzyme-Linked Immunosorbent Assay (ELISA) using peptides, primary antibody dilutions between 1:20000 to 1:40000 are commonly used. It is important to note that these dilutions are approximate ranges and may need to be optimized for specific experiments.

Immunogen

A synthesized peptide derived from human MDM2.

Properties

Concentration

1mg/ml

Purification

We employed SulfoLink™ Coupling Resin for peptide affinity chromatography to purify the antiserum.

Clonality

Polyclonal Antibody

Stability & Storage

It is recommended to keep the product at -20 °C for a duration of one year without undergoing repeated freeze/thaw cycles.

Storage buffer

The rabbit IgG solution is formulated in a pH 7.4 phosphate buffered saline with 150mM NaCl, 0.02% sodium azide, and 50% glycerol for optimal stability. This solution should be stored at -20 °C and is guaranteed to remain stable for up to 12 months from date of receipt.

Target

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 (PubMed:12821780, PubMed:15053880, PubMed:15195100, PubMed:15632057, PubMed:16337594, PubMed:17290220, PubMed:19098711, PubMed:19219073, PubMed:19837670, PubMed:19965871, PubMed:20173098, PubMed:20385133, PubMed:20858735, PubMed:22128911). Ubiquitinates DCX, leading to DCX degradation and reduction of the dendritic spine density of olfactory bulb granule cells (By similarity).

Tissue specificity

Ubiquitous. Isoform Mdm2-A, isoform Mdm2-B, isoform Mdm2-C, isoform Mdm2-D, isoform Mdm2-E, isoform Mdm2-F and isoform Mdm2-G are observed in a range of cancers but absent in normal tissues.

Posttranslational modification

Phosphorylation on Ser-166 by SGK1 activates ubiquitination of p53/TP53. Phosphorylated at multiple sites near the RING domain by ATM upon DNA damage; this prevents oligomerization and E3 ligase processivity and impedes constitutive p53/TP53 degradation.Autoubiquitination leads to proteasomal degradation; resulting in p53/TP53 activation it may be regulated by SFN. Also ubiquitinated by TRIM13. Deubiquitinated by USP2 leads to its accumulation and increases deubiquitination and degradation of p53/TP53. Deubiquitinated by USP7 leading to its stabilization.

Celluar localization

Cytosol;Nucleus;Plasma Membrane;

UniPort

Q00987