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|Application ||IHC-P, E|
|Calculated MW||42547 Da|
|Other Names||Cell cycle checkpoint control protein RAD9A, hRAD9, DNA repair exonuclease rad9 homolog A, RAD9A|
|Target/Specificity||This RAD9 Antibody is generated from rabbits immunized with a KLH conjugated synthetic phosphopeptide corresponding to amino acid residues surrounding S387 of human RAD9.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Phospho-RAD9(S387) Antibody is for research use only and 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.|
Provided below are standard protocols that you may find useful for product applications.
Rad9 is highly similar to Schizosaccharomyces pombe rad9, a cell cycle checkpoint protein required for cell cycle arrest and DNA damage repair in response to DNA damage. This protein is found to possess 3' to 5' exonuclease activity, which may contribute to its role in sensing and repairing DNA damage. It forms a checkpoint protein complex with RAD1 and HUS1. This complex is recruited by checkpoint protein RAD17 to the sites of DNA damage, which is thought to be important for triggering the checkpoint-signaling cascade.
Maniwa, Y., et al., Cancer 103(1):126-132 (2005). Wang, W., et al., Proc. Natl. Acad. Sci. U.S.A. 101(48):16762-16767 (2004). Lindsey-Boltz, L.A., et al., (er) Nucleic Acids Res. 32(15):4524-4530 (2004). Toueille, M., et al., (er) Nucleic Acids Res. 32(11):3316-3324 (2004). Loegering, D., et al., J. Biol. Chem. 279(18):18641-18647 (2004).