RAD9, Antibody

EC 3.1.11.2; RAD9A; RADIO-resistance/CHEMO-resistance/cell cycle checkpoint control protein

For Research Use Only. Not for use in diagnostic procedures.

RAD9 antibody detects endogenous levels of total RAD9 protein.

Affinity-purified fromrabbit antiserum by affinity-chromatography using epitope-specific immunogen.

In phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.

Store at-20 degree C for 1 year.

Small volumes of anti-RAD9 antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Immunohistochemistry (IHC), ELISA (EIA)

IHC: 1:50-1:100
ELISA: 1:5000

Peptide-+ Immunohistochemistry analysis of paraffin-embedded human lung carcinoma tissue using RAD9 antibody.

42,547 Da

RAD9 checkpoint clamp component A

cell cycle checkpoint control protein RAD9A

Cell cycle checkpoint control protein RAD9A

hRAD9  [Similar Products]

This gene product is highly similar to Schizosaccharomyces pombe rad9, a cell cycle checkpoint protein required for cell cycle arrest and DNA damage repair. This protein possesses 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. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Aug 2011]

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.

Pia Roos-Mattjus, J. Biol. Chem., Jun 2003; 278: 24428-24437. Kiyotsugu Yoshida, Mol. Cell. Biol., May 2002; 22: 3292-3300. Haiying Hang, Nucleic Acids Res., Nov 2000; 28: 4340-4349.

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