BRCA1 (E5S9G) Rabbit mAb #50799
- WB
- IP
- IHC
- IF
Supporting Data
| REACTIVITY | H Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 220 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
- IHC-Immunohistochemistry
- IF-Immunofluorescence
Species Cross-Reactivity Key:
- H-Human
- Mk-Monkey
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:50 |
| IHC Leica Bond | 1:150 - 1:600 |
| Immunohistochemistry (Paraffin) | 1:150 - 1:600 |
| Immunofluorescence (Immunocytochemistry) | 1:50 - 1:200 |
Storage
For a carrier free (BSA and azide free) version of this product see product #20225.
Protocol
Specificity / Sensitivity
BRCA1 (E5S9G) Rabbit mAb recognizes endogenous levels of total BRCA1 protein. Non-specific staining of kidney tubules was observed by immunohistochemistry.
Species Reactivity:
Human, Monkey
Source / Purification
Monoclonal antibody is produced by immunizing animals with recombinant protein specific to the carboxy terminus of human BRCA1 protein.
Background
The breast cancer susceptibility proteins BRCA1 and BRCA2 are frequently mutated in cases of hereditary breast and ovarian cancers and have roles in multiple processes related to DNA damage, repair, cell cycle progression, transcription, ubiquitination, and apoptosis (1-4). BRCA2 has been shown to be required for localization of Rad51 to sites of double-stranded breaks (DSBs) in DNA, and cells lacking BRCA1 and BRCA2 cannot repair DSBs through the Rad51-dependent process of homologous recombination (HR) (5). Numerous DNA damage-induced phosphorylation sites on BRCA1 have been identified, including Ser988, 1189, 1387, 1423, 1457, 1524, and 1542, and kinases activated in a cell cycle-dependent manner, including Aurora A and CDK2, can also phosphorylate BRCA1 at Ser308 and Ser1497, respectively (6-10). Cell cycle-dependent phosphorylation of BRCA2 at Ser3291 by CDKs has been proposed as a mechanism to switch off HR as cells progress beyond S-phase by blocking the carboxy-terminal Rad51 binding site (11).
- Rahman, N. and Stratton, M.R. (1998) Annu Rev Genet 32, 95-121.
- Gayther, S.A. et al. (1999) Am J Hum Genet 65, 1021-9.
- Kerr, P. and Ashworth, A. (2001) Curr Biol 11, R668-76.
- Scully, R. and Livingston, D.M. (2000) Nature 408, 429-32.
- Tutt, A. and Ashworth, A. (2002) Trends Mol Med 8, 571-6.
- Okada, S. and Ouchi, T. (2003) J Biol Chem 278, 2015-20.
- Cortez, D. et al. (1999) Science 286, 1162-6.
- Xu, B. et al. (2002) Cancer Res 62, 4588-91.
- Ouchi, M. et al. (2004) J Biol Chem 279, 19643-8.
- Ruffner, H. et al. (1999) Mol Cell Biol 19, 4843-54.
- Esashi, F. et al. (2005) Nature 434, 598-604.
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