ExactAntigen

RPA2 antibody | antibody review based on formal publications
RPA2 antibodies
This is a review about RPA2 antibodies, based on 4 published articles using RPA2 antibodies in western blot, immunohistochemistry, immunoprecipitation, immunocytochemistry, and other immunological technologies. It is aimed to help ExactAntigen visitors find the most suited RPA2 antibody.
EMD Biosciences    search EMD Biosciences RPA2 products
ic, wbOncogene Research Products anti-RPA2 antibody was used in western blot and immunocytochemistry to study the role of protein phosphatase 5 in ATR-mediated checkpoint activation. to the paper
icOncogene Research Products monoclonal anti-RPA2 antibody RPA34-20 was used in immunocytochemistry to study the 32-kDa subunit (RPA2) of replication protein A (RPA) interaction with menin. to the paper
NEOMARKERS
ip, wbNeoMarkers anti-RPA p34 (9H8) antibody was used in western blot and immunoprecipitations to study the role of amino-terminal domain of ATRIP intranuclear relocation of the ATR-ATRIP complex following DNA damage. to the paper
wbNeoMarkers mouse monoclonal antibody against RPA2 was used in western blot to study the formation of nucleolin-p53 complex. to the paper
LAB VISION CORPORATION
emsa, ic, ip, wbLab Vision Corporation monoclonal antibody against RPA2 (SSB34A) was used in western blot, immunoprecipitation, EMSA and immunocytochemistry to study the 32-kDa subunit (RPA2) of replication protein A (RPA) interaction with menin. to the paper
Articles Reviewed
1:Ji Zhang et al. Protein phosphatase 5 is required for ATR-mediated checkpoint activation. 2005
2:Eisuke Itakura et al. Amino-terminal domain of ATRIP contributes to intranuclear relocation of the ATR-ATRIP complex following DNA damage. 2004
3:Karen E Sukhodolets et al. The 32-kilodalton subunit of replication protein A interacts with menin, the product of the MEN1 tumor suppressor gene. 2003
4:Yaron Daniely et al. Stress-dependent nucleolin mobilization mediated by p53-nucleolin complex formation. 2002


2008©ExactAntigen home | browse | about