|Other Names||Cell cycle checkpoint control protein RAD9A, hRAD9, DNA repair exonuclease rad9 homolog A, RAD9A|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||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. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase. RAD9A possesses 3'->5' double stranded DNA exonuclease activity. Its phosphorylation by PRKCD may be required for the formation of the 9-1-1 complex.|
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This gene product is highly similar to Schizosaccharomycespombe rad9, a cell cycle checkpoint protein required for cell cyclearrest and DNA damage repair in response to DNA damage. Thisprotein is found to possess 3' to 5' exonuclease activity, whichmay contribute to its role in sensing and repairing DNA damage. Itforms a checkpoint protein complex with RAD1 and HUS1. This complexis recruited by checkpoint protein RAD17 to the sites of DNAdamage, which is thought to be important for triggering thecheckpoint-signaling cascade. Use of alternative polyA sites hasbeen noted for this gene.
Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)Takeishi, Y., et al. Genes Cells 15(7):761-771(2010)Greer Card, D.A., et al. J. Biol. Chem. 285(20):15653-15661(2010)Bai, H., et al. DNA Repair (Amst.) 9(5):478-487(2010)Sierant, M.L., et al. Cell Cycle 9(3):548-556(2010)
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