Rad1 [4126]

4126

Amino terminal fragment of human Rad1 purified from E. coli.

HeLa whole cell lysate

Nuclear

From mouse ascitic fluid Storage

For WB: Use at a dilution of 1:1 000. Detects a band of approximately 28 kDa (predicted

28 kDa Cellular

Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3\' -OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double nick or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. Isoform 1 possesses 3\' -& gt; 5\' double stranded DNA exonuclease activity.

Component of the toroidal 9-1-1 (RAD9-RAD1-HUS1) complex composed of RAD9A RAD1 and HUS1. The 9-1-1 complex associates with LIG1 POLB FEN1 RAD17 HDAC1 RPA1 and RPA2. The 9-1-1 complex associates with the RAD17-RFC complex. RAD1 interacts with POLB FEN1 HUS1 HUS1B RAD9A and RAD9B.

Expressed in testis uterus bladder spleen ovaries lung brain and muscle (at protein level).