Rabbit Anti-p53 Polyclonal Antibody #abs130596

abs130596-50ug

1-2 Weeks

201

abs130596-100ug

1-2 Weeks

301

Description

The nuclear protein tumor protein p53 is a crucial regulator of the cell cycle, particularly during the transition from G0 to G1. In most normal cells, p53 is present in low amounts, whereas in various transformed cell lines, it is expressed at elevated levels and is thought to contribute to transformation and malignancy. P53 is a DNA-binding protein that contains domains for DNA-binding, oligomerization, and transcription activation. It is believed to bind as a tetramer to a p53-binding site and trigger the expression of downstream genes that hinder growth and/or invasion, thus acting as a tumor suppressor. Mutations in the p53 gene that occur commonly in different cancers in humans fail to bind to the consensus DNA binding site, thus leading to the loss of tumor suppressor activity. TP53 gene alterations arise not only as somatic mutations in human cancers but also as germline mutations in some cancer-prone families with Li-Fraumeni syndrome.

Other names

P53, also known as tumor protein 53 or cellular tumor antigen p53, is an important protein involved in tumor suppression. It is encoded by the TP53 gene and is widely recognized for its role in maintaining genomic stability and preventing the formation of cancerous cells. Mutations in the TP53 gene can lead to the production of a mutant form of p53, which can contribute to the development of various types of cancer. P53 is classified as a phosphoprotein due to its high level of phosphorylation. It has been shown to regulate the expression of numerous genes involved in cell cycle arrest, DNA repair, apoptosis, and senescence. The importance of p53 in tumor suppression is evident by its association with several genetic disorders, such as Li-Fraumeni syndrome (LFS1), where individuals inherit a defective copy of the TP53 gene. The function of p53 as a tumor suppressor has significant implications in cancer research and therapeutics.

Source

Rabbit

Specificity

p53 Antibody detects endogenous levels of p53.

Species Reactivity

Human;Mouse;Rat

Application

ELISA (peptide) has a dilution range of 1:20000-1:40000, while IF/ICC has a dilution range of 1:100-1:500. IHC, on the other hand, has a dilution range of 1:50-1:200. Lastly, WB has the widest dilution range, which is 1:500-1:2000. It is important to note that these dilution ranges refer to the recommended concentrations for each assay.

Immunogen

A synthesized peptide derived from human p53.

Properties

Concentration

1mg/ml

Purification

SulfoLink™ Coupling Resin was employed to conduct peptide affinity chromatography and purify the antiserum. This procedure resulted in the production of a highly purified antiserum for further use.

Clonality

Polyclonal Antibody

Stability & Storage

To maintain its quality, the product should be stored at a temperature of -20 °C for a period of one year. It is essential to avoid subjecting it to multiple freeze/thaw cycles.

Storage buffer

The storage conditions for Rabbit IgG are as follows: it should be stored at a temperature of -20 °C. The formulation of the solution includes phosphate buffered saline at a pH of 7.4, with the addition of 150mM NaCl, 0.02% sodium azide, and 50% glycerol. It is important to note that this product has a shelf life of 12 months from the date of receipt.

Target

Background

Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. Induces the transcription of long intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA-p21 participates in TP53-dependent transcriptional repression leading to apoptosis and seem to have to effect on cell-cycle regulation. Implicated in Notch signaling cross-over. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression. Isoform 2 enhances the transactivation activity of isoform 1 from some but not all TP53-inducible promoters. Isoform 4 suppresses transactivation activity and impairs growth suppression mediated by isoform 1. Isoform 7 inhibits isoform 1-mediated apoptosis. Regulates the circadian clock by repressing CLOCK-ARNTL/BMAL1-mediated transcriptional activation of PER2 (PubMed:24051492).

Tissue specificity

Ubiquitous. Isoforms are expressed in a wide range of normal tissues but in a tissue-dependent manner. Isoform 2 is expressed in most normal tissues but is not detected in brain, lung, prostate, muscle, fetal brain, spinal cord and fetal liver. Isoform 3 is expressed in most normal tissues but is not detected in lung, spleen, testis, fetal brain, spinal cord and fetal liver. Isoform 7 is expressed in most normal tissues but is not detected in prostate, uterus, skeletal muscle and breast. Isoform 8 is detected only in colon, bone marrow, testis, fetal brain and intestine. Isoform 9 is expressed in most normal tissues but is not detected in brain, heart, lung, fetal liver, salivary gland, breast or intestine.

Posttranslational modification

Acetylated. Acetylation of Lys-382 by CREBBP enhances transcriptional activity. Deacetylation of Lys-382 by SIRT1 impairs its ability to induce proapoptotic program and modulate cell senescence. Deacetylation by SIRT2 impairs its ability to induce transcription activation in a AKT-dependent manner.Phosphorylation on Ser residues mediates transcriptional activation. Phosphorylated by HIPK1 (By similarity). Phosphorylation at Ser-9 by HIPK4 increases repression activity on BIRC5 promoter. Phosphorylated on Thr-18 by VRK1. Phosphorylated on Ser-20 by CHEK2 in response to DNA damage, which prevents ubiquitination by MDM2. Phosphorylated on Ser-20 by PLK3 in response to reactive oxygen species (ROS), promoting p53/TP53-mediated apoptosis. Phosphorylated on Thr-55 by TAF1, which promotes MDM2-mediated degradation. Phosphorylated on Ser-33 by CDK7 in a CAK complex in response to DNA damage. Phosphorylated on Ser-46 by HIPK2 upon UV irradiation. Phosphorylation on Ser-46 is required for acetylation by CREBBP. Phosphorylated on Ser-392 following UV but not gamma irradiation. Phosphorylated on Ser-15 upon ultraviolet irradiation; which is enhanced by interaction with BANP. Phosphorylated by NUAK1 at Ser-15 and Ser-392; was initially thought to be mediated by STK11/LKB1 but it was later shown that it is indirect and that STK11/LKB1-dependent phosphorylation is probably mediated by downstream NUAK1 (PubMed:21317932). It is unclear whether AMP directly mediates phosphorylation at Ser-15. Phosphorylated on Thr-18 by isoform 1 and isoform 2 of VRK2. Phosphorylation on Thr-18 by isoform 2 of VRK2 results in a reduction in ubiquitination by MDM2 and an increase in acetylation by EP300. Stabilized by CDK5-mediated phosphorylation in response to genotoxic and oxidative stresses at Ser-15, Ser-33 and Ser-46, leading to accumulation of p53/TP53, particularly in the nucleus, thus inducing the transactivation of p53/TP53 target genes. Phosphorylated by DYRK2 at Ser-46 in response to genotoxic stress. Phosphorylated at Ser-315 and Ser-392 by CDK2 in response to DNA-damage.Dephosphorylated by PP2A-PPP2R5C holoenzyme at Thr-55. SV40 small T antigen inhibits the dephosphorylation by the AC form of PP2A.May be O-glycosylated in the C-terminal basic region. Studied in EB-1 cell line.Ubiquitinated by MDM2 and SYVN1, which leads to proteasomal degradation (PubMed:10722742, PubMed:12810724, PubMed:15340061, PubMed:17170702, PubMed:19880522). Ubiquitinated by RFWD3, which works in cooperation with MDM2 and may catalyze the formation of short polyubiquitin chains on p53/TP53 that are not targeted to the proteasome (PubMed:10722742, PubMed:12810724, PubMed:20173098). Ubiquitinated by MKRN1 at Lys-291 and Lys-292, which leads to proteasomal degradation (PubMed:19536131). Deubiquitinated by USP10, leading to its stabilization (PubMed:20096447). Ubiquitinated by TRIM24, RFFL, RNF34 and RNF125, which leads to proteasomal degradation (PubMed:19556538). Ubiquitination by TOPORS induces degradation (PubMed:19473992). Deubiquitination by USP7, leading to stabilization (PubMed:15053880). Isoform 4 is monoubiquitinated in an MDM2-independent manner (PubMed:15340061). Ubiquitinated by RFWD2, which leads to proteasomal degradation (PubMed:19837670). Ubiquitination and subsequent proteasomal degradation is negatively regulated by CCAR2 (PubMed:25732823).Monomethylated at Lys-372 by SETD7, leading to stabilization and increased transcriptional activation. Monomethylated at Lys-370 by SMYD2, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity. Lys-372 monomethylation prevents interaction with SMYD2 and subsequent monomethylation at Lys-370. Dimethylated at Lys-373 by EHMT1 and EHMT2. Monomethylated at Lys-382 by KMT5A, promoting interaction with L3MBTL1 and leading to repress transcriptional activity. Dimethylation at Lys-370 and Lys-382 diminishes p53 ubiquitination, through stabilizing association with the methyl reader PHF20. Demethylation of dimethylated Lys-370 by KDM1A prevents interaction with TP53BP1 and represses TP53-mediated transcriptional activation.Sumoylated with SUMO1. Sumoylated at Lys-386 by UBC9.

Celluar localization

Cytosol;Endoplasmic reticulum;Mitochondrion;Nucleus;

UniPort

P04637