Mouse monoclonal antibody raised against synthetic peptide of acetylated histones and TP53.
A synthetic acetylated peptide (conjugated with KLH) corresponding to residues surrounding Lys382 of human TP53.
Quality Control Testing:
The Acetylated Histone/p53-K382 Monoclonal Antibody (TM-5C5) detects endogenous acetylated Histones and several acetylated protein including acetylated p53 (acetylated lysine 382). The antibody does not recognize non-acetylated Histone nor non-acetylated p53.
Western Blot (1-2 ug/mL) Immunofluorescence (5-10 ug/mL) ELISA (0.5-1 ug/mL) The optimal working dilution should be determined by the end user.
In 10 mM phosphate buffer, 150 mM NaCl, pH 7.2 (50% glycerol)
Store at -20°C. Aliquot to avoid repeated freezing and thawing.
Western blot analysis of extracts from MRC-5 cells or SAOS-2 cells that had been treated with 10 uM Cycloheximide or 1 uM Trichostatin A for 12 hours using the Acetylated Histone/p53-K382 monoclonal antibody, clone TM-5C5 (Cat # MAB0018).
Immunofluorescence detection of Acetylated-Histone in MRC-5 cells after treatment of 1 uM Trichostatin A or vehicle (DMSO) for 4 hours using the Acetylated Histone/p53-K382 monoclonal antibody, clone TM-5C5 (Cat # MAB0018).
ELISA for measuring level of cellular histone acetylation after treatment of Trichostain A using Acetylated Histone/p53-K382 monoclonal antibody, clone TM-5C5 (Cat # MAB0018).
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
p53 antigen,p53 transformation suppressor,p53 tumor suppressor,phosphoprotein p53,transformation-related protein 53