A new set of monoclonal antibodies directed to proline-rich and central regions of p53
Morel, A. P.
Rostan, M. C.
De Fromentel, C. C.
Hybridoma and Hybridomics
Mary Ann Liebert, Inc.
287 - 292
Item Usage Stats
MetadataShow full item record
The p53 protein can adopt several conformations in cells - "latent," "active," or mutant - depending on cellular stress or mutations of the TP53 gene. Today, only a few antibodies discriminating these conformations are available. We produced three new anti-p53 monoclonal antibodies (MAbs) directed against epitopes of human p53. The H53C1 MAb recognizes an epitope located at the N-terminal part of the central region of p53 and can discriminate mutant from wild-type conformation. The H53C2 and H53C3 MAbs are against different epitopes within the proline-rich region of p53. Moreover, the H53C2 epitope is located in the second negative regulatory domain of p53 between residues 80 and 93. These MAbs can be used as new tools to study and modulate the cellular functions of p53.
monoclonal antibody h53c1
monoclonal antibody h53c2
Monoclonal antibody h53c3
Amino terminal sequence
Published Version (Please cite this version)http://dx.doi.org/10.1089/hyb.2004.23.287
Showing items related by title, author, creator and subject.
Nuclear exclusion of p33ING1b tumor suppressor protein: explored in HCC cells using a new highly specific antibody Sayan, B.; Emre, N. C. T.; Irmak, M. B.; Ozturk, M.; Cetin Atalay, R. (Mary Ann Liebert, Inc, 2009)Mouse monoclonal antibodies (MAb) were generated against p33ING1b tumor suppressor protein. 15B9 MAb was highly specific in recognizing a single protein band of ∼33 kDa endogenous p33ING1b protein from HCC cell lines and ...
Yolcu, E.; Sayan, B. S.; Yağci, T.; Cetin Atalay, R.; Soussi, T.; Yurdusev, N.; Ozturk, M. (Nature Publishing Group, 2001)Three monoclonal antibodies (Mabs) were generated against p53 DNA-binding core domain. When tested by immunoprecipitation, Western blot and immunofluorescence techniques, Mab 9E4, as well as 7D3 and 6B10 reacted with both ...