Mouse Rad9a Blocking Peptide (N-term)
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | Q9Z0F6 |
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Gene ID | 19367 |
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Other Names | Cell cycle checkpoint control protein RAD9A, mRAD9, DNA repair exonuclease rad9 homolog A, Rad9-like protein, Rad9a, Rad9 |
Target/Specificity | The synthetic peptide sequence is selected from aa 29-42 of HUMAN Rad9a |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
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. |
Name | Rad9a |
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Synonyms | Rad9 |
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. |
Cellular Location | Nucleus {ECO:0000250|UniProtKB:Q99638}. |
Tissue Location | Expressed in heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis. |
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Background
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 (By similarity).
References
Hang H.,et al.J. Cell. Physiol. 177:241-247(1998).
Carninci P.,et al.Science 309:1559-1563(2005).
Park Y.-G.,et al.Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
Ishii H.,et al.Proc. Natl. Acad. Sci. U.S.A. 102:9655-9660(2005).
Sweet S.M.,et al.Mol. Cell. Proteomics 8:904-912(2009).
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