Thermo Fisher Scientific p53 Monoclonal Antibody (Y5)

Applications

Tested Dilution

Publications

Western Blot (WB)

1:250

-

Immunohistochemistry (IHC)

-

View 1 publication 1 publication

Immunohistochemistry (Paraffin) (IHC (P))

1:100

View 1 publication 1 publication

Immunocytochemistry (ICC/IF)

1:250

-

Product Specifications

Published species

Human

Host/Isotype

Rabbit / IgG

Class

Monoclonal

Type

Antibody

Clone

Y5

Immunogen

A synthetic peptide derived from N- terminal residues of human p53 if (typeof window.$mangular === undefined || !window.$mangular) { window.$mangular = {}; } $mangular.antigenJson = \[{targetFamily:p53,uniProtId:P04637-1,ncbiNodeId:9606,antigenRange:1,antigenLength:393,antigenImageFileName:MA5-14467_p53_P04637-1_Rabbit.svg,antigenImageFileNamePDP:MA5-14467_p53_P04637-1_Rabbit_PDP.jpeg,sortOrder:1}\]; $mangular.isB2BCMGT = false; $mangular.isEpitopesModalImageMultiSizeEnabled = true;

View immunogen .st0{fill:#FFFFFF;} .st1{fill:#1E8AE7;}

Conjugate

Unconjugated Unconjugated Unconjugated

Form

Liquid

Concentration

Conc. Not Determined

Storage conditions

4° C

Shipping conditions

Wet ice

RRID

AB_10978647

Product Specific Information

MA5-14467 targets p53 in IHC (P) applications and shows reactivity with Human samples.

The MA5-14467 immunogen is a synthetic peptide derived from N- terminal residues of human p53.

Target Information

The tumor suppressor protein, p53, is a sequence specific transcription factor that is activated by cellular stress. p53 mediates cell cycle arrest or apoptosis in response to DNA damage or starvation for pyrimidine nucleotides. p53 is up-regulated in response to stress signals and stimulated to activate transcription of specific genes, resulting in expression of p21waf1 and other proteins involved in G1 or G2/M arrest. The structure of p53 comprises an N-terminal transactivation domain, a central DNA-binding domain, an oligomerisation domain, and a C-terminal regulatory domain. There are various phosphorylation sites on p53, of which the phosphorylation at Ser15 is important for p53 activation and stabilization. p53 has been characterized to play a role in blocking the proliferative action of damaged cells and act as an anticancer agent. Phosphorylation of Ser392 in p53 has been shown to associate with the formation of human tumors. In addition, p53 has also been linked to the effects of aging and oxidative stress and an increase in p53 has been linked to deficits in LTP (Long Term Potentiation) in learning and memory. p53 is found in very low levels in normal cells, however, in a variety of transformed cell lines, it is expressed in high amounts, and believed to contribute to transformation and malignancy. Mutants of p53 that frequently occur in a number of different human cancers fail to bind the consensus DNA binding site, and cause the loss of tumor suppressor activity. Alterations of the TP53 gene occur not only as somatic mutations in human malignancies, but also as germline mutations in some cancer-prone families such as Li-Fraumeni syndrome.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.