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Mdm2 Antibody (C-term)

Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - Mdm2 Antibody (C-term) AP1254a
    All lanes : Anti-MDM2 Antibody (C-term) at 1:1000 dilution Lane 1: CCRF-CEM whole cell lysate Lane 2: MCF-7 whole cell lysate Lane 3: A549 whole cell lysate Lane 4: Daudi whole cell lysate Lane 5: Jurkat whole cell lysate Lysates/proteins at 20 µg per lane. Secondary Goat Anti-Rabbit IgG, (H+L), Peroxidase conjugated at 1/10000 dilution. Predicted band size : 55 kDa Blocking/Dilution buffer: 5% NFDM/TBST.
  • 14 - Mdm2 Antibody (C-term) AP1254a
    Mdm2 Antibody (C-term) (Cat.#AP1254a) immunohistochemistry analysis in formalin fixed and paraffin embedded human prostate carcinoma followed by peroxidase conjugation of the secondary antibody and DAB staining. This data demonstrates the use of the Mdm2 Antibody (C-term) for immunohistochemistry. Clinical relevance has not been evaluated.
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  • 文献引用 : 5
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Product info
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, IHC-P, E
Primary Accession Q00987
Reactivity Human
Host Rabbit
Clonality Polyclonal
Isotype Rabbit Ig
Additional info
Gene ID 4193
Other Names E3 ubiquitin-protein ligase Mdm2, 632-, Double minute 2 protein, Hdm2, Oncoprotein Mdm2, p53-binding protein Mdm2, MDM2
Target/Specificity This Mdm2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 393-424 amino acids from the C-terminal region of human Mdm2.
Dilution WB~~1:1000
IHC-P~~1:10~50
Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein G column, eluted with high and low pH buffers and neutralized immediately, followed by dialysis against PBS.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsMdm2 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.
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 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.
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
Research Areas
Introduction of the MDM2 T309G Mutation in Primary Human Retinal Epithelial Cells Enhances Experimental Proliferative Vitreoretinopathy.
Author : Zhou G1,2,Duan Y1,2,Ma G1,3,Wu W1,Hu Z1,Chen N1,Chee Y4,Cui J5,Samad A6,Matsubara JA5,Mukai S4,D'Amore PA1,Lei H1.
Invest Ophthalmol Vis Sci. 2017 Oct 1;58(12):5361-5367. doi: 10.1167/iovs.17-22045.
29049737
The Clustered, Regularly Interspaced, Short Palindromic Repeats-associated Endonuclease 9 (CRISPR/Cas9)-created MDM2 T309G Mutation Enhances Vitreous-induced Expression of MDM2 and Proliferation and Survival of Cells.
Author : Duan Y1, Ma G2, Huang X2, D\'Amore PA3, Zhang F4, Lei H5.
J Biol Chem. 2016 Jul 29;291(31):16339-47. doi: 10.1074/jbc.M116.729467. Epub 2016 May 31.
27246850
P53-Derived peptides conjugation to PEI: an approach to producing versatile and highly efficient targeted gene delivery carriers into cancer cells.
Author : Mokhtarzadeh A1,2,3, Parhiz H2, Hashemi M4, Abnous K2, Ramezani M2,4.
Expert Opin Drug Deliv. 2015 Dec 10. [Epub ahead of print]
26654047
RASSF10 suppresses colorectal cancer growth by activating P53 signaling and sensitizes colorectal cancer cell to docetaxel.
Author : Guo J1, Yang Y1,2, Yang Y1, Linghu E1, Zhan Q3, Brock MV4, Herman JG4, Zhang B5, Guo M1.
Oncotarget. 2015 Feb 28;6(6):4202-13.
25638156
The deubiquitinating enzyme USP2a regulates the p53 pathway by targeting Mdm2.
Author : Stevenson LF, Sparks A, Allende-Vega N, Xirodimas DP, Lane DP, Saville MK.
EMBO J. 2007 Feb 21;26(4):976-86. Epub 2007 Feb 8.
17290220

BACKGROUND

MDM2 is a target of the transcription factor tumor protein p53. The encoded protein is a nuclear phosphoprotein that binds 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 protein p53, diminishing its tumor suppressor function. This protein has E3 ubiquitin ligase activity, which targets tumor protein p53 for proteasomal degradation. This protein 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).

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