Phospho-Ser392 p53 Antibody
Affinity purified rabbit polyclonal antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB |
---|---|
Primary Accession | P04637 |
Reactivity | Rat |
Predicted | Human |
Host | Rabbit |
Clonality | polyclonal |
Calculated MW | 53 KDa |
Gene ID | 7157 |
---|---|
Gene Name | TP53 |
Other Names | Cellular tumor antigen p53, Antigen NY-CO-13, Phosphoprotein p53, Tumor suppressor p53, TP53, P53 |
Target/Specificity | Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser392 conjugated to KLH. |
Dilution | WB~~ 1:1000 |
Format | Prepared from rabbit serum by affinity purification via sequential chromatography on phospho- and dephosphopeptide affinity columns. |
Antibody Specificity | Specific for the ~53k p53 protein phosphorylated at Ser392. The immunolabeling is completely eliminated by λ-phosphatase treatment. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | Phospho-Ser392 p53 Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
Shipping | Blue Ice |
- Primary Antibodies
- Cancer
- Cell Biology
- Microbiology
- Signal Transduction
- Antibody Collections
- Amyotrophic Lateral Sclerosis (ALS)
- Phospho Antibodies
- SARS-Human interaction partners
- Necrosis
- Necroptosis
- Mitochondrion
- Apoptosis signaling
- Apoptosis
- Host-virus interaction
- Viral process
- Anti-Wnt-Pathway (plus Lgr5) Antibodies
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Provided below are standard protocols that you may find useful for product applications.
Background
p53 has a well established role in blocking the proliferative action of damaged cells and acting in essence as an anticancer agent (Sharpless and DePinho, 2002; Yin et al., 1992). It has been called the guardian of the genome (Lane, 1992). Phosphorylation of Ser392 in p53 is associated with formation of human tumors (Saito et al., 2003; Pise-Masison et al., 1998; Kim et al., 2004). In addition, p53 has been linked to effects of aging and oxidative stress (Sharpless and DePinho, 2002). An increase in p53 has also been linked to deficits in LTP and learning and memory (Jiang et al., 1998).
References
Jiang YH, Armstrong D, Albrecht U, Atkins CM, Noebels JL, Eichele G, Sweatt JD, Beaudet AL (1998) Mutation of the angelman ubiquitin ligase in mice causes increased cytoplasmic p53 and deficits of contextual learning and long-term potentiation. Neuron 21:799-811.
Kim YY, Park BJ, Kim DJ, Kim WH, Kim S, Oh KS, Lim JY, Kim J, Park C, Park SI (2004) Modification of serine 392 is a critical event in the regulation of p53 nuclear export and stability. FEBS Lett 572:92-98.
Lane DP (1992) p53, guardian of the genome. Nature (London) 358:15-16.
Pise-Masison CA, Radonovich M, Sakaguchi K, Appella E, Brady JN (1998) Phosphorylation of p53: a novel pathway for p53 inactivation in human T- cell lymphotropic virus type 1-transformed cells. J Virol 72:6348-6355.
Saito S, Yamaguchi H, Higashimoto Y, Chao C, Xu Y, Fornace AJ, Jr., Appella E, Anderson CW (2003) Phosphorylation site interdependence of human p53 post-translational modifications in response to stress. J Biol Chem 278:37536-37544.
Sharpless NE, DePinho RA (2002) p53: Good cop/bad cop. Cell 110:9-12.
Yin Y, Tainsky MA, Bischoff FZ, Strong LC, Wahl GM (1992) Wild-type p53 restores cell cycle control and inhibits gene amplification in cells with mutant p53 alleles. Cell 70:937-948.
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