Product Pathways - Chromatin Regulation / Epigenetics
SMARCD3/BAF60C (D6F1S) Rabbit mAb #62265
|62265S||100 µl ( 10 western blots )||￥3,250.00 现货查询||购买询价|
|62265||carrier free & custom formulation / quantity||email request|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IP=Immunoprecipitation,
Specificity / Sensitivity
SMARCD3/BAF60A (D6F1S) Rabbit mAb recognizes endogenous levels of total SMARCD3/BAF60C protein.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human SMARCD3/BAF60C protein.
ATP-dependent chromatin remodeling complexes play an essential role in the regulation of nuclear processes such as transcription and DNA replication and repair (1,2). The SWI/SNF chromatin remodeling complex consists of more than 10 subunits and contains a single molecule of either BRM or BRG1 as the ATPase catalytic subunit. The activity of the ATPase subunit disrupts histone-DNA contacts and changes the accessibility of crucial regulatory elements to the chromatin. The additional core and accessory subunits play a scaffolding role to maintain stability and provide surfaces for interaction with various transcription factors and chromatin (2-5). The interactions between SWI/SNF subunits and transcription factors, such as nuclear receptors, p53, Rb, BRCA1, and MyoD, facilitate recruitment of the complex to target genes for regulation of gene activation, cell growth, cell cycle, and differentiation processes (1,6-9).
SMARCD3/BAF60C is essential for the development of the skeletal and cardiac muscle (10,11). Knockdown of SMARCD3/BAF60C using RNAi in mouse embryos leads to defects in heart development as well as abnormalities in the development of the cardiac and skeletal muscle, mimicking the cardiac defects observed in congenital heart disease (12). In addition, SMARCD3/BAF60C is part of the lipoBAF complex that remodels the chromaitn structure to activate lipogenic genes, promoting lipogenesis in response to feeding and insulin (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.
- Puri, P.L. and Mercola, M. (2012) Genes Dev 26, 2673-83.
- Vallaster, M. et al. (2012) Acta Biochim Biophys Sin (Shanghai) 44, 92-102.
- Lickert, H. et al. (2004) Nature 432, 107-12.
- Wang, Y. et al. (2013) Mol Cell 49, 283-97.
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For Research Use Only. Not For Use In Diagnostic Procedures.
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