RAD1 Antibody (N-Terminus, clone 4126)
Mouse Monoclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, IHC-P |
---|---|
Primary Accession | O60671 |
Reactivity | Human |
Host | Mouse |
Clonality | Monoclonal |
Clone Names | 4126 |
Calculated MW | 32kDa |
Dilution | IHC-P (10 µg/ml) |
Gene ID | 5810 |
---|---|
Other Names | Cell cycle checkpoint protein RAD1, hRAD1, 3.1.11.2, DNA repair exonuclease rad1 homolog, Rad1-like DNA damage checkpoint protein, RAD1, REC1 |
Target/Specificity | Amino terminal fragment of human Rad1 purified from E. coli. |
Reconstitution & Storage | Long term: -20°C; Short term: +4°C. Avoid repeat freeze-thaw cycles. |
Precautions | RAD1 Antibody (N-Terminus, clone 4126) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | RAD1 |
---|---|
Synonyms | REC1 |
Function | Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair (PubMed:10846170, PubMed:10884395). The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex (PubMed:12578958). Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER) (PubMed:15871698). 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 (PubMed:15314187, PubMed:15556996, PubMed:15871698). The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase (PubMed:21659603). |
Cellular Location | Nucleus. |
Tissue Location | Expressed in testis, uterus, bladder, spleen, ovaries, lung, brain and muscle (at protein level) |
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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. Isoform 1 possesses 3'->5' double stranded DNA exonuclease activity.
References
Freire R.,et al.Genes Dev. 12:2560-2573(1998).
Bluyssen H.A.R.,et al.Genomics 54:331-337(1998).
Marathi U.K.,et al.Genomics 54:344-347(1998).
Dean F.B.,et al.Genomics 54:424-436(1998).
Parker A.E.,et al.J. Biol. Chem. 273:18332-18339(1998).
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