TP53 polyclonal antibody
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Specification
Product Description
Rabbit polyclonal antibody raised against synthetic peptide of TP53.
Immunogen
A synthetic peptide corresponding to residues surrounding S6 of human TP53.
Host
Rabbit
Reactivity
Human
Specificity
This antibody is specific to TP53.
Form
Liquid
Purification
Affinity purification
Concentration
1 mg/mL
Recommend Usage
Western Blot (1:500-1:1000)
Immunohistochemistry (1:50-1:100)
ELISA (1:20000)
The optimal working dilution should be determined by the end user.Storage Buffer
In PBS, 150mM NaCl, pH 7.4 (50% glycerol, 0.02% sodium azide)
Storage Instruction
Store at -20°C.
Aliquot to avoid repeated freezing and thawing.Note
This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
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Applications
Western Blot (Cell lysate)
Western blot analysis of extracts from MDA-MB-435 cells (Lane 1 and 2) and 293 (Lane 3) using TP53 polyclonal antibody (Cat # PAB18494).
Peptide "+" means "peptide blocking".Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections)
Immunohistochemical analysis of paraffin-embedded human breast carcinoma tissue using TP53 polyclonal antibody (Cat # PAB18494).
Peptide "+" means "peptide blocking".Enzyme-linked Immunoabsorbent Assay
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Gene Info — TP53
Entrez GeneID
7157Protein Accession#
P04637Gene Name
TP53
Gene Alias
FLJ92943, LFS1, TRP53, p53
Gene Description
tumor protein p53
Gene Ontology
HyperlinkGene Summary
This gene encodes tumor protein p53, which responds to diverse cellular stresses to regulate target genes that induce cell cycle arrest, apoptosis, senescence, DNA repair, or changes in metabolism. p53 protein is expressed at low level in normal cells and at a high level in a variety of transformed cell lines, where it's believed to contribute to transformation and malignancy. p53 is a DNA-binding protein containing transcription activation, DNA-binding, and oligomerization domains. It is postulated to bind to a p53-binding site and activate expression of downstream genes that inhibit growth and/or invasion, and thus function as a tumor suppressor. Mutants of p53 that frequently occur in a number of different human cancers fail to bind the consensus DNA binding site, and hence cause the loss of tumor suppressor activity. Alterations of this gene occur not only as somatic mutations in human malignancies, but also as germline mutations in some cancer-prone families with Li-Fraumeni syndrome. Multiple p53 variants due to alternative promoters and multiple alternative splicing have been found. These variants encode distinct isoforms, which can regulate p53 transcriptional activity. [provided by RefSeq
Other Designations
p53 antigen|p53 transformation suppressor|p53 tumor suppressor|phosphoprotein p53|transformation-related protein 53
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Interactome
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Pathway
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Disease
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Publication Reference
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Glycogen synthase kinase-3 interacts with and phosphorylates estrogen receptor alpha and is involved in the regulation of receptor activity.
Medunjanin S, Hermani A, De Servi B, Grisouard J, Rincke G, Mayer D.
The Journal of Biological Chemistry 2005 Aug; 280(38):33006.
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Phosphorylation of p53 on key serines is dispensable for transcriptional activation and apoptosis.
Thompson T, Tovar C, Yang H, Carvajal D, Vu BT, Xu Q, Wahl GM, Heimbrook DC, Vassilev LT.
The Journal of Biological Chemistry 2004 Oct; 279(51):53015.
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Limited role of N-terminal phosphoserine residues in the activation of transcription by p53.
Jackson MW, Agarwal MK, Agarwal ML, Agarwal A, Stanhope-Baker P, Williams BR, Stark GR.
Oncogene 2004 May; 23(25):4477.
Application:WB, Human, NARF2, U-2 OS cells.
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Ligand-independent interactions of p160/steroid receptor coactivators and CREB-binding protein (CBP) with estrogen receptor-alpha: regulation by phosphorylation sites in the A/B region depends on other receptor domains.
Dutertre M, Smith CL.
Molecular Endocrinology (Baltimore, Md.) 2003 Apr; 17(7):1296.
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Activation of estrogen receptor alpha by S118 phosphorylation involves a ligand-dependent interaction with TFIIH and participation of CDK7.
Chen D, Riedl T, Washbrook E, Pace PE, Coombes RC, Egly JM, Ali S.
Molecular Cell 2000 Jul; 6(1):127.
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Glycogen synthase kinase-3 interacts with and phosphorylates estrogen receptor alpha and is involved in the regulation of receptor activity.
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