Rad51

The p53-binding protein 1 (53BP1) is a DNA damage response factor, which is recruited to nuclear structures at the site of DNA damage.  DNA double-strand breaks (DSBs) are mutations that are detrimental to cell viability and genome stability, and must be repaired either through homologous recombination (HR) or non-homologous end joining (NHEJ). 53BP1 specifically promotes both NHEJ as well as the inhibition of HR repair, yet the decision making on a molecular level between these two routes not clearly understood.

RAD51 is a recombinase protein encoded by RAD51 gene in humans. Human RAD51 family members are highly similar to bacterial RecA and yeast Rad51, both biochemically and structurally. It is a 339-amino acid protein that plays an important role in homologous recombination (HR) of DNA during double-strand break (DSB) repair.

Mediating DNA damage is a crucial process, and one of the most important cellular guards against cancer. In response to DNA damage, sophisticated cellular machinery is recruited to repair the breaks, and if it fails, the cell is committed to death.

The DMC1 gene encodes a 36.7 kDa nuclear protein involved in meiotic homologous recombination. This recombinase is functionally related to the yeast RAD51 and E. coli RecA genes. In contrast to RAD51, which functions in both mitotic and meiotic recombination, DMC1 works specifically in meiotic recombination. Despite this difference, the RAD51 and DMC1 recombinase are structurally similar but not identical in nature.

Our antibody catalog includes an extensive range of Rad51 antibody reagents. Encoded by the RAD51 gene, the Rad51 protein plays a vital role in DNA repair, interacting with several other proteins, including BRCA1 and BRCA2, to effect homologous recombination at double-strand breaks.

Human cancer research is the largest research area in our antibody database, with new oncogenes and cell lines being added all the time.