Rabbit anti-Human p53 Polyclonal Antibody | anti-TP53 antibody

Anti-p53 Antibody, Rabbit Polyclonal

Cat. Num. AAA8100033

• Reactivity: Human
• Applications: Western Blot
• Purity: Protein A & Antigen Affinity
• Synonyms: p53; Polyclonal Antibody; Anti-p53 Antibody; Rabbit Polyclonal; P53 Antibody; Rabbit PAb; Antigen Affinity Purified; tumor protein p53; Anti-BCC7 Antibody; Anti-LFS1 Antibody; Anti-P53 Antibody; Anti-TRP53 Antibody; anti-TP53 antibody

• Host: Rabbit
• Reactivity: Human
• Clonality: Polyclonal
• Isotype: Rabbit IgG
• Specificity: Human P53 phosphorylated at Ser392
• Purity/Purification: Protein A & Antigen Affinity
• Form/Format: Liquid; 0.2um filtered solution in PBS

• Applicable Applications for anti-TP53 antibody: Western Blot (WB)
• Application Notes: WB: 1:500-1:2000
• Immunogen: A synthetic phospho-peptide corresponding to residues surrounding Ser392 of human P53
• Conjugation: Unconjugated
• Preparation: Produced in rabbits immunized with A synthetic phospho-peptide corresponding to residues surrounding Ser392 of human P53., and purified by antigen affinity chromatography.
• Preparation and Storage: This antibody can be stored at 2-8 degree C for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20 degree C to -80 degree C. Preservative-Free. Avoid repeated freeze-thaw cycles.

Western Blot (WB)

(Anti-P53 rabbit polyclonal antibody at 1:500 dilution.Lane A: HepG2 Whole Cell LysateLane B: MV-1-LUtreated with 20mM hydroxyurea for 30hLysates/proteins at 30 ug per lane.SecondaryGoat Anti-Rabbit IgG H&L (Dylight800) at 1/10000 dilution.Developed using the Odyssey technique. Performed under reducing conditions.Predicted band size:53 kDaObserved band size:53 kDa)

Related Product Information for anti-TP53 antibody

p53, also known as Tp53, is a DNA-binding protein which belongs to the p53 family. It contains transcription activation, DNA-binding, and oligomerization domains. 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 (TP53) is a transcription factor whose protein levels and post-translational modification state alter in response to cellular stress (such as DNA damage, hypoxia, spindle damage). Activation of p53 begins through a number of mechanisms including phosphorylation by ATM, ATR, Chk1 and MAPKs. MDM2 is a ubiquitin ligase that binds p53 and targets p53 for proteasomal degradation. Phosphorylation, p14ARF and USP7 prevent MDM2-p53 interactions, leading to an increase in stable p53 tetramers in the cytoplasm. Further modifications such as methylation and acetylation lead to an increase in Tp53 binding to gene specific response elements. Tp53 regulates a large number of genes (>100 genes) that control a number of key tumor suppressing functions such as cell cycle arrest, DNA repair, senescence and apoptosis. Whilst the activation of p53 often leads to apoptosis, p53 inactivation facilitates tumor progression. 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. Defects in TP53 are a cause of esophageal cancer, Li-Fraumeni syndrome, lung cancer and adrenocortical carcinoma.

Product Categories/Family for anti-TP53 antibody

Apoptosis Transcription Factors and Regulators Cancer Drug Targets Tumor Suppressors; Death Receptor Signaling

References

Bakhrat A, et al. (2010) Drosophila Chk2 and p53 proteins induce stage-specific cell death independently during oogenesis. Apoptosis. 15(12):1425-34.
Kurzhals RL, et al. (2011) Chk2 and p53 are haploinsufficient with dependent and independent functions to eliminate cells after telomere loss. PLoS Genet. 7(6):e1002103.
Pardi N, et al. (2011) In vivo effects of abolishing the single canonical sumoylation site in the C-terminal region of Drosophila p53. Acta Biol Hung. 62(4):397-412.
Wells BS, et al. (2012) Maintenance of imaginal disc plasticity and regenerative potential in Drosophila by p53. Dev Biol. 361(2):263-76.