BARD1 Antibody (aa108-124)
Rabbit Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| IHC-P, E |
---|---|
Primary Accession | Q99728 |
Reactivity | Human |
Host | Rabbit |
Clonality | Polyclonal |
Calculated MW | 87kDa |
Dilution | ELISA (1:1000), IHC-P (10 µg/ml), |
Gene ID | 580 |
---|---|
Other Names | BRCA1-associated RING domain protein 1, BARD-1, 6.3.2.-, BARD1 |
Target/Specificity | Amino acids 108 to 124 of human BARD1 |
Reconstitution & Storage | Long term: -20°C; Short term: +4°C. Avoid repeat freeze-thaw cycles. |
Precautions | BARD1 Antibody (aa108-124) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | BARD1 |
---|---|
Function | E3 ubiquitin-protein ligase. The BRCA1-BARD1 heterodimer specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Plays a central role in the control of the cell cycle in response to DNA damage. Acts by mediating ubiquitin E3 ligase activity that is required for its tumor suppressor function. Also forms a heterodimer with CSTF1/CSTF-50 to modulate mRNA processing and RNAP II stability by inhibiting pre-mRNA 3' cleavage. |
Cellular Location | Nucleus. Note=During S phase of the cell cycle, colocalizes with BRCA1 into discrete subnuclear foci. Can translocate to the cytoplasm. Localizes at sites of DNA damage at double-strand breaks (DSBs); recruitment to DNA damage sites is mediated by the BRCA1-A complex |
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Background
Probable E3 ubiquitin-protein ligase. The BRCA1-BARD1 heterodimer specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Plays a central role in the control of the cell cycle in response to DNA damage. Acts by mediating ubiquitin E3 ligase activity that is required for its tumor suppressor function. Also forms a heterodimer with CSTF1/CSTF-50 to modulate mRNA processing and RNAP II stability by inhibiting pre-mRNA 3' cleavage.
References
Wu L.C.,et al.Nat. Genet. 14:430-440(1996).
Thai T.H.,et al.Hum. Mol. Genet. 7:195-202(1998).
Li L.,et al.Cancer Res. 67:11876-11885(2007).
Hillier L.W.,et al.Nature 434:724-731(2005).
Meza J.E.,et al.J. Biol. Chem. 274:5659-5665(1999).
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