SWAP70 polyclonal antibody

SWAP-70 is a protein that is part of a protein complex that catalyzes cell-free DNA recombination between immunoglobulin (Ig) heavy chain gene switch region substrates. In resting B lymphocytes, SWAP-70 is localized mainly in the cytoplasm, however, in activated B cells, SWAP-70 is recruited to the plasma membrane and then translocates to the nucleus. In the nucleus, SWAP-70 recognizes specific switch regions, acting as a switch recombinase and causing a DNA break. The cellular and intracellular localization before and after B-cell activation also suggests a role for SWAP-70 in signaling in B cell activation. In addition, SWAP-70 contains three nuclear localization signals, has a weak affinity for DNA, binds ATP, and forms specific, high affinity complexes with B23, C23, and poly (ADP-ribose) polymerase.