Product Datasheet  
RPA32/RPA2 (Phospho-phospho T21) Antibody  
Catalog Number: 13390  
Technical:tech@swbio.com  
Information:info@swbio.com  
Description  
  • host_species：  
  • Rabbit
  • Amount：  
  • 100μgμg
  • Swiss-Prot No.：  
  • Swiss-Prot#:P15927
  • Form of Antibody：  
  • 1*TBS (pH7.4), 1%BSA, 40%Glycerol. Preservative: 0.05% Sodium Azide.
  • Storage：  
  • Store at -20˚C
  • Immunogen：  
  • Synthetic phospho-peptide corresponding to residues surrounding Thr21 of human RPA32/RPA2.
  • reactivity：  
  • Hu, Ms, Rt
  • appl_detail：  
  • WB: 1:1,000



  • other_names：  
  • 60S acidic ribosomal protein P1 antibody
    AA409079 antibody
    AI325195 antibody
    AU020965 antibody
    ik:tdsubc_2g1 antibody
    M(2)21C antibody
    MGC137236 antibody
    OTTHUMP00000004008 antibody
    p32 antibody
  • Purification：  
  • ProA affinity purified
  • Specificity：  
  • Applications：  
  • WB, IP
  • Background：  
  • The single-stranded-DNA-binding proteins (SSBs) are essential for DNA function in prokaryotic and eukaryotic cells, mitochondria, phages and viruses. Replication protein A (RPA), a highly conserved eukaryotic protein, is a heterotrimeric SSB. RPA plays an important role in DNA replication, recombination and repair. The binding of human RPA (hRPA) to DNA involves molecular polarity in which initial hRPA binding occurs on the 5' side of a ssDNA substrate and then extends in the 3' direction to create a stably bound hRPA. RPA is a major damage-recognition protein involved in the early stages of nucleotide excision repair. It can also play a role in telomere maintenance. The C-terminus of RPA 32 can specfically intereact with the DNA repair enzyme UNG2 and repair factors XPA and Rad52, each of which functions in a different repair pathway. In addition, RPA 32 binds specifically to the SH2 domain of Stat3 in vivo, and overexpression of RPA 32 corresponds to the augmented growth factor-stimulated tyrosine phosphorylation and transcription activities of Stat3.



 
© Signalway Biotechnology All Rights Reserved.