The p53 gene is mutated in approximately half of all human cancers. It is involved in the cellular response to cytotoxic stresses, and together with p19ARF, induces expression of p21Cip1, to cause cell cycle arrest. In addition, p53 is able to induce apoptosis, both by transcriptional and non-transcriptional mechanisms. The amino-terminal 83 amino acids of p53 contain the transactivation domain, as well as the region involved in transcription-independent growth suppression. The carboxy-terminal region contains the DNA-binding domain, which is regulated by three phosphorylation events, and potentially by acetylation also.
Product Information
Format
Unpurified
Presentation
Unpurified rabbit monoclonal IgG in buffer containing 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.
Applications
Application
Use Anti-phospho-p53 (Ser392) Antibody, clone EP155Y (rabbit monoclonal antibody) validated in IHC(P), ICC, IP, WB to detect phospho-p53 (Ser392) also known as Antigen NY-CO-13 ,Phosphoprotein p53, Tumor suppressor p53, p53 antigen.
Key Applications
Western Blotting
Immunohistochemistry (Paraffin)
Immunocytochemistry
Immunoprecipitation
Application Notes
Immunohistochemistry (Paraffin) Analysis:
Anti-phospho-p53 (Ser392) was diluted to 1:200.
Immunofluorescent Immunocytochemistry:
Cells were stained with anti-phopsho-p53 (Ser392) at a 1:250 dilution.
Immunoprecipitation:
A 1:50 dilution of a previous lot was used in IP.
Biological Information
Immunogen
Synthetic peptide corresponding to phosphorylated Ser392 and surrounding amino acids of human p53.
Epitope
Phosphorylated Ser392
Clone
EP155Y
Host
Rabbit
Specificity
This antibody recognizes p53 when phosphorylated on Ser392.
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].
FUNCTION: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. Ref.48
Cofactor Binds 1 zinc ion per subunit.
SUBUNIT STRUCTURE:Interacts with AXIN1. Probably part of a complex consisting of TP53, HIPK2 and AXIN1 By similarity. Binds DNA as a homotetramer. Interacts with histone acetyltransferases EP300 and methyltransferases HRMT1L2 and CARM1, and recruits them to promoters. In vitro, the interaction of TP53 with cancer-associated/HPV (E6) viral proteins leads to ubiquitination and degradation of TP53 giving a possible model for cell growth regulation. This complex formation requires an additional factor, E6-AP, which stably associates with TP53 in the presence of E6. C-terminus interacts with TAF1, when TAF1 is part of the TFIID complex. Interacts with ING4 and this interaction may be indirect. Found in a complex with CABLES1 and TP73. Interacts with HIPK1, HIPK2, and P53DINP1. Interacts with WWOX. May interacts with HCV core protein. Interacts with USP7 and SYVN1. Interacts with HSP90AB1. Interacts with CHD8, leading to recruit histone H1 and prevent transactivation activity By similarity. Interacts with ARMC10, BANP, CDKN2AIP and E4F1.
DOMAIN:The nuclear export signal acts as a transcriptional repression domain. Ref.34
PTM: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.
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, which may prevent the interaction with MDM2. Phosphorylated on Thr-55 by TAF1, which promotes MDM2-mediated degradation. 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 upon DNA damage, probably by ATM or ATR. Phosphorylated on Ser-15 upon ultraviolet irradiation; which is enhanced by interaction with BANP.
Dephosphorylated by PP2A. SV40 small T antigen inhibits the dephosphorylation by the AC form of PP2A. Ref.51 Ref.24 Ref.26 Ref.31 Ref.35 Ref.36 Ref.40 Ref.41 Ref.49 Ref.53 Ref.58 Ref.59 Ref.60
May be O-glycosylated in the C-terminal basic region. Studied in EB-1 cell line. Ref.28
Ubiquitinated by SYVN1, which leads to proteasomal degradation. Ref.56
Monomethylated at Lys-372 by SETD7, leading to stabilize it and increase transcriptional activation. Monomethylated at Lys-370 by SMYD2, leading to decrease DNA-binding activity and subsequent transcriptional regulation activity. Lys-372 monomethylation prevents the interaction with SMYD2 and subsequenct monomethylation at Lys-370. Ref.50 Ref.54 Ref.55
DISEASE:TP53 is found in increased amounts in a wide variety of transformed cells. TP53 is frequently mutated or inactivated in about 60% of cancers.
Defects in TP53 are involved in esophageal squamous cell carcinoma (ESCC) [MIM:133239]. ESCC is a tumor of the esophagus.
Defects in TP53 are a cause of Li-Fraumeni syndrome (LFS) [MIM:151623]. LFS is an autosomal dominant familial cancer syndrome that in its classic form is defined by the existence of a proband affected by a sarcoma before 45 years with a first degree relative affected by any tumor before 45 years and another first degree relative with any tumor before 45 years or a sarcoma at any age. Other clinical definitions for LFS have been proposed (Ref.95 and Ref.98) and called Li-Fraumeni like syndrome (LFL). In these families affected relatives develop a diverse set of malignancies at unusually early ages. Four types of cancers account for 80% of tumors occurring in TP53 germline mutation carriers: breast cancers, soft tissue and bone sarcomas, brain tumors (astrocytomas) and adrenocortical carcinomas. Less frequent tumors include choroid plexus carcinoma or papilloma before the age of 15, rhabdomyosarcoma before the age of 5, leukemia, Wilms tumor, malignant phyllodes tumor, colorectal and gastric cancers. Ref.74 Ref.75 Ref.76 Ref.77 Ref.78 Ref.97 Ref.99 Ref.104 Ref.105
Defects in TP53 may be associated with nasopharyngeal carcinoma [MIM:161550]; also known as nasopharyngeal cancer.
Defects in TP53 are found in Barrett metaplasia; also known as Barrett esophagus. It is a condition in which the normally stratified squamous epithelium of the lower esophagus is replaced by a metaplastic columnar epithelium. The condition develops as a complication in approximately 10% of patients with chronic gastroesophageal reflux disease and predisposes to the development of esophageal adenocarcinoma.
Defects in TP53 are involved in head and neck squamous cell carcinomas (HNSCC) [MIM:275355].
Defects in TP53 are involved in oral squamous cell carcinoma (OSCC). Cigarette smoke is a prime mutagenic agent in cancer of the aerodigestive tract.
Defects in TP53 are a cause of lung cancer [MIM:211980].
Defects in TP53 are a cause of choroid plexus papilloma [MIM:260500]. Choroid plexus papilloma is a slow-growing benign tumor of the choroid plexus that often invades the leptomeninges. In children it is usually in a lateral ventricle but in adults it is more often in the fourth ventricle. Hydrocephalus is common, either from obstruction or from tumor secretion of cerebrospinal fluid. If it undergoes malignant transformation it is called a choroid plexus carcinoma. Primary choroid plexus tumors are rare and usually occur in early childhood. Ref.108
Defects in TP53 are a cause of one form of hereditary adrenocortical carcinoma (ADCC) [MIM:202300]. ADCC is a rare childhood tumor, representing about 0.4% of childhood tumors, with a high incidence of associated tumors. ADCC occurs with increased frequency in patients with the Beckwith-Wiedemann syndrome [MIM:130650] and is a component tumor in Li-Fraumeni syndrome [MIM:151623]. Ref.107
SIMILARITY:Belongs to the p53 family.
Product Usage Statements
Quality Assurance
Routinely evaluated by Western Blot in lysate from A431 treated with Calyculin A and Okadaic acid.
Western Blot Analysis:
A 1:500 dilution of this antibody was used to detect p53 phosphorylated on Ser392 in A431 treated with Calyculin A and Okadaic acid.
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Storage and Shipping Information
Storage Conditions
Stable for 1 year at -20ºC from date of receipt.
Handling Recommendations: Upon receipt, and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance. Note: Variability in freezer temperatures below -20°C may cause glycerol containing solutions to become frozen during storage.
The p53 gene is mutated in approximately half of all human cancers. It is involved in the cellular response to cytotoxic stresses, and together with p19ARF, induces expression of p21Cip1, to cause cell cycle arrest. In addition, p53 is able to induce apoptosis, both by transcriptional and non-transcriptional mechanisms. The amino-terminal 83 amino acids of p53 contain the transactivation domain, as well as the region involved in transcription-independent growth suppression. The carboxy-terminal region contains the DNA-binding domain, which is regulated by three phosphorylation events, and potentially by acetylation also.
Product Information
Format
Unpurified
Presentation
Unpurified rabbit monoclonal IgG in buffer containing 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.
Applications
Application
Use Anti-phospho-p53 (Ser392) Antibody, clone EP155Y (rabbit monoclonal antibody) validated in IHC(P), ICC, IP, WB to detect phospho-p53 (Ser392) also known as Antigen NY-CO-13 ,Phosphoprotein p53, Tumor suppressor p53, p53 antigen.
Key Applications
Western Blotting
Immunohistochemistry (Paraffin)
Immunocytochemistry
Immunoprecipitation
Application Notes
Immunohistochemistry (Paraffin) Analysis:
Anti-phospho-p53 (Ser392) was diluted to 1:200.
Immunofluorescent Immunocytochemistry:
Cells were stained with anti-phopsho-p53 (Ser392) at a 1:250 dilution.
Immunoprecipitation:
A 1:50 dilution of a previous lot was used in IP.
Biological Information
Immunogen
Synthetic peptide corresponding to phosphorylated Ser392 and surrounding amino acids of human p53.
Epitope
Phosphorylated Ser392
Clone
EP155Y
Host
Rabbit
Specificity
This antibody recognizes p53 when phosphorylated on Ser392.
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].
FUNCTION: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. Ref.48
Cofactor Binds 1 zinc ion per subunit.
SUBUNIT STRUCTURE:Interacts with AXIN1. Probably part of a complex consisting of TP53, HIPK2 and AXIN1 By similarity. Binds DNA as a homotetramer. Interacts with histone acetyltransferases EP300 and methyltransferases HRMT1L2 and CARM1, and recruits them to promoters. In vitro, the interaction of TP53 with cancer-associated/HPV (E6) viral proteins leads to ubiquitination and degradation of TP53 giving a possible model for cell growth regulation. This complex formation requires an additional factor, E6-AP, which stably associates with TP53 in the presence of E6. C-terminus interacts with TAF1, when TAF1 is part of the TFIID complex. Interacts with ING4 and this interaction may be indirect. Found in a complex with CABLES1 and TP73. Interacts with HIPK1, HIPK2, and P53DINP1. Interacts with WWOX. May interacts with HCV core protein. Interacts with USP7 and SYVN1. Interacts with HSP90AB1. Interacts with CHD8, leading to recruit histone H1 and prevent transactivation activity By similarity. Interacts with ARMC10, BANP, CDKN2AIP and E4F1.
DOMAIN:The nuclear export signal acts as a transcriptional repression domain. Ref.34
PTM: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.
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, which may prevent the interaction with MDM2. Phosphorylated on Thr-55 by TAF1, which promotes MDM2-mediated degradation. 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 upon DNA damage, probably by ATM or ATR. Phosphorylated on Ser-15 upon ultraviolet irradiation; which is enhanced by interaction with BANP.
Dephosphorylated by PP2A. SV40 small T antigen inhibits the dephosphorylation by the AC form of PP2A. Ref.51 Ref.24 Ref.26 Ref.31 Ref.35 Ref.36 Ref.40 Ref.41 Ref.49 Ref.53 Ref.58 Ref.59 Ref.60
May be O-glycosylated in the C-terminal basic region. Studied in EB-1 cell line. Ref.28
Ubiquitinated by SYVN1, which leads to proteasomal degradation. Ref.56
Monomethylated at Lys-372 by SETD7, leading to stabilize it and increase transcriptional activation. Monomethylated at Lys-370 by SMYD2, leading to decrease DNA-binding activity and subsequent transcriptional regulation activity. Lys-372 monomethylation prevents the interaction with SMYD2 and subsequenct monomethylation at Lys-370. Ref.50 Ref.54 Ref.55
DISEASE:TP53 is found in increased amounts in a wide variety of transformed cells. TP53 is frequently mutated or inactivated in about 60% of cancers.
Defects in TP53 are involved in esophageal squamous cell carcinoma (ESCC) [MIM:133239]. ESCC is a tumor of the esophagus.
Defects in TP53 are a cause of Li-Fraumeni syndrome (LFS) [MIM:151623]. LFS is an autosomal dominant familial cancer syndrome that in its classic form is defined by the existence of a proband affected by a sarcoma before 45 years with a first degree relative affected by any tumor before 45 years and another first degree relative with any tumor before 45 years or a sarcoma at any age. Other clinical definitions for LFS have been proposed (Ref.95 and Ref.98) and called Li-Fraumeni like syndrome (LFL). In these families affected relatives develop a diverse set of malignancies at unusually early ages. Four types of cancers account for 80% of tumors occurring in TP53 germline mutation carriers: breast cancers, soft tissue and bone sarcomas, brain tumors (astrocytomas) and adrenocortical carcinomas. Less frequent tumors include choroid plexus carcinoma or papilloma before the age of 15, rhabdomyosarcoma before the age of 5, leukemia, Wilms tumor, malignant phyllodes tumor, colorectal and gastric cancers. Ref.74 Ref.75 Ref.76 Ref.77 Ref.78 Ref.97 Ref.99 Ref.104 Ref.105
Defects in TP53 may be associated with nasopharyngeal carcinoma [MIM:161550]; also known as nasopharyngeal cancer.
Defects in TP53 are found in Barrett metaplasia; also known as Barrett esophagus. It is a condition in which the normally stratified squamous epithelium of the lower esophagus is replaced by a metaplastic columnar epithelium. The condition develops as a complication in approximately 10% of patients with chronic gastroesophageal reflux disease and predisposes to the development of esophageal adenocarcinoma.
Defects in TP53 are involved in head and neck squamous cell carcinomas (HNSCC) [MIM:275355].
Defects in TP53 are involved in oral squamous cell carcinoma (OSCC). Cigarette smoke is a prime mutagenic agent in cancer of the aerodigestive tract.
Defects in TP53 are a cause of lung cancer [MIM:211980].
Defects in TP53 are a cause of choroid plexus papilloma [MIM:260500]. Choroid plexus papilloma is a slow-growing benign tumor of the choroid plexus that often invades the leptomeninges. In children it is usually in a lateral ventricle but in adults it is more often in the fourth ventricle. Hydrocephalus is common, either from obstruction or from tumor secretion of cerebrospinal fluid. If it undergoes malignant transformation it is called a choroid plexus carcinoma. Primary choroid plexus tumors are rare and usually occur in early childhood. Ref.108
Defects in TP53 are a cause of one form of hereditary adrenocortical carcinoma (ADCC) [MIM:202300]. ADCC is a rare childhood tumor, representing about 0.4% of childhood tumors, with a high incidence of associated tumors. ADCC occurs with increased frequency in patients with the Beckwith-Wiedemann syndrome [MIM:130650] and is a component tumor in Li-Fraumeni syndrome [MIM:151623]. Ref.107
SIMILARITY:Belongs to the p53 family.
Product Usage Statements
Quality Assurance
Routinely evaluated by Western Blot in lysate from A431 treated with Calyculin A and Okadaic acid.
Western Blot Analysis:
A 1:500 dilution of this antibody was used to detect p53 phosphorylated on Ser392 in A431 treated with Calyculin A and Okadaic acid.
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Storage and Shipping Information
Storage Conditions
Stable for 1 year at -20ºC from date of receipt.
Handling Recommendations: Upon receipt, and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance. Note: Variability in freezer temperatures below -20°C may cause glycerol containing solutions to become frozen during storage.
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