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Phospho-MDM2-pS166 Antibody Blocking PeptideSynthetic peptide
| Country | United States
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| Catalog # | Size | Availability | Price | |
| BP3501a | 0.1 mg 400 ul | In Stock | $ 45.00 | DISCONTINED INQUIRE CLICK INQUIRE Add to cart |
- Specification
- Citiations : 0
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- Backgrounds
Phospho-MDM2-pS166 Antibody Blocking Peptide - Product info | |
| Primary Accession | Q00987 |
| Clone Names | 5022853 |
| Calculated MW | 55233 Da |
Phospho-MDM2-pS166 Antibody Blocking Peptide - Additional info | |
| Gene ID 4193 | |
| Target/Specificity The synthetic peptide sequence used to generate the antibody AP3501a was selected from the region of human Phospho-MDM2-pT166. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. | |
| Format Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml. | |
| Storage Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. | |
| Precautions This product is for research use only. Not for use in diagnostic or therapeutic procedures. | |
Phospho-MDM2-pS166 Antibody Blocking Peptide - Protein Information | |
| Name MDM2 | |
| Function 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 an 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 | |
| Cellular Location Nucleus, nucleoplasm. Cytoplasm. Nucleus, nucleolus. Note=Expressed predominantly in the nucleoplasm Interaction with ARF(P14) results in the localization of both proteins to the nucleolus. The nucleolar localization signals in both ARF(P14) and MDM2 may be necessary to allow efficient nucleolar localization of both proteins. Colocalizes with RASSF1 isoform A in the nucleus | |
| Tissue Location 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 | |
Phospho-MDM2-pS166 Antibody Blocking Peptide - Related products
AP1253a: Mdm2 Antibody (N-term)
AP1254a: Mdm2 Antibody (C-term)
AP3490a: Phospho-MDM2-T218 Antibody
AP3501a: Phospho-MDM2-pS166 Antibody
AP3579a: Phospho-MDM2-pS395 Antibody
BP1253a: Mdm2 Antibody (N-term) Blocking Peptide
BP1253d: MDM2 Antibody (T218) Blocking Peptide
BP1253e: MDM2 Antibody (S166) Blocking Peptide
BP1254a: Mdm2 Antibody (C-term) Blocking Peptide
BP3490a: Phospho-MDM2-T218 Antibody Blocking Peptide
BP3501a: Phospho-MDM2-pS166 Antibody Blocking Peptide
Phospho-MDM2-pS166 Antibody Blocking Peptide - Research Areas
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BACKGROUND
MDM2 is a target of the transcription factor tumor protein p53. It is a nuclear phosphoprotein that binds to and inhibits transactivation by tumor protein p53, as part of an autoregulatory negative feedback loop. Overexpression of MDM2 can result in excessive inactivation of tumor proteinp53, diminishing its tumor suppressor function. This protein has E3ubiquitin ligase activity, which targets tumor protein p53 for proteasomal degradation. It also affects the cell cycle,apoptosis, and tumorigenesis through interactions with other proteins, including retinoblastoma 1 and ribosomal protein L5.
REFERENCES
Burch, L.R., et al., J. Mol. Biol. 337(1):115-128 (2004).Schon, O., et al., J. Mol. Biol. 336(1):197-202 (2004).Mantesso, A., et al., J. Oral Pathol. Med. 33(2):96-101 (2004).Shmueli, A., et al., Mol. Cell 13(1):4-5 (2004).Xia, L., et al., Cancer Res. 64(1):221-228 (2004).
