Brg1 (D1Q7F) Rabbit mAb #49360
- WB
- IP
- ChIP
- C&R
Supporting Data
| REACTIVITY | H M R Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 220 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
- ChIP-Chromatin Immunoprecipitation
- C&R-CUT & RUN
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Mk-Monkey
Product Information
Product Usage Information
The CUT&RUN dilution was determined using CUT&RUN Assay Kit #86652.
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:100 |
| Chromatin IP | 1:50 |
| Chromatin IP-seq | 1:50 |
| CUT&RUN | 1:50 |
Storage
Protocol
Specificity / Sensitivity
Brg1 (D1Q7F) Rabbit mAb recognizes endogenous levels of total Brg1 protein. This antibody does not cross-react with BRM protein.
Species Reactivity:
Human, Mouse, Rat, Monkey
Source / Purification
Monoclonal antibody is produced by immunizing animals with recombinant protein specific to the amino terminus of human Brg1 protein.
Background
ATP-dependent chromatin remodeling complexes play an essential role in the regulation of various nuclear processes, such as gene expression, DNA replication, and repair (1,2). The SWI/SNF chromatin remodeling complex consists of more than 10 subunits with a single molecule of the ATPase catalytic subunit BRM or BRG1, but not both. The activities of these two subunits drive the disruption of histone-DNA contacts that lead to changes in accessibility of crucial regulatory elements within chromatin (2-5). The BRM/BRG1 containing SWI/SNF complexes are recruited to target promoters by transcription factors, such as nuclear receptors, p53, RB, and BRCA1 to regulate gene activation, cell growth, the cell cycle, and differentiation processes (1,6-9). BRM and BRG1 are also considered to be tumor suppressors and their expression levels are severely reduced in several cancer cell lines (10-13).
- Ho, L. and Crabtree, G.R. (2010) Nature 463, 474-84.
- Becker, P.B. and Hörz, W. (2002) Annu Rev Biochem 71, 247-73.
- Eberharter, A. and Becker, P.B. (2004) J Cell Sci 117, 3707-11.
- Bowman, G.D. (2010) Curr Opin Struct Biol 20, 73-81.
- Gangaraju, V.K. and Bartholomew, B. (2007) Mutat Res 618, 3-17.
- Lessard, J.A. and Crabtree, G.R. (2010) Annu Rev Cell Dev Biol 26, 503-32.
- Morettini, S. et al. (2008) Front Biosci 13, 5522-32.
- Wolf, I.M. et al. (2008) J Cell Biochem 104, 1580-6.
- Simone, C. (2006) J Cell Physiol 207, 309-14.
- Yamamichi, N. et al. (2005) Oncogene 24, 5471-81.
- Reisman, D.N. et al. (2002) Oncogene 21, 1196-207.
- Shen, H. et al. (2008) Cancer Res 68, 10154-62.
- Weissman, B. and Knudsen, K.E. (2009) Cancer Res 69, 8223-30.
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