Product Pathways - Chromatin Regulation / Epigenetics
SMARCA1 Antibody #9450
PhosphoSitePlus® protein, site, and accession data: SMARCA1
| Applications | Reactivity | Sensitivity | MW (kDa) | Source |
|---|---|---|---|---|
| W IP | H | Endogenous | 130 | Rabbit |
Applications Key:
W=Western Blotting
IP=Immunoprecipitation
Reactivity Key:
H=Human
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Protocols
Specificity / Sensitivity
SMARCA1 Antibody recognizes endogenous levels of total SMARCA1 protein.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human SMARCA1 protein. Antibodies are purified by protein A and peptide affinity chromatography.
Background
SMARCA1 (SNF2L) is one of the two orthologs of the ISWI (imitation switch) ATPases encoded by the mammalian genome (1). The ISWI chromatin remodeling complexes were first identified in Drosophila and have been shown to remodel and alter nucleosome spacing in vitro (2). SMARCA1 is the catalytic subunit of the nucleosome remodeling factor (NURF) and CECR2-containing remodeling factor (CERF) complexes (3-5). The NURF complex plays an important role in neuronal physiology by promoting neurite outgrowth and regulation of Engrailed homeotic genes that are involved in neuronal development in the mid-hindbrain (3). NURF is also thought to be involved in the maturation of T cells from thymocytes by regulating chromatin structure and expression of genes important for T cell development (6). The largest subunit of the NURF complex, BPTF, is required for proper development of mesoderm, endoderm, and ectoderm tissue lineages, suggesting a role for SMARCA1 in the development of the germ layers in mouse embryo (7). Disruption of the CERF complex by deletion of CECR2, an interacting partner of SMARCA1, is associated with the neural tube defect exencephaly, linking the CERF complex with regulation of neurulation (4).
- Lazzaro, M.A. and Picketts, D.J. (2001) J Neurochem 77, 1145-56.
- Erdel, F. and Rippe, K. (2011) FEBS J 278, 3608-18.
- Barak, O. et al. (2003) EMBO J 22, 6089-100.
- Banting, G.S. et al. (2005) Hum Mol Genet 14, 513-24.
- Ho, L. and Crabtree, G.R. (2010) Nature 463, 474-84.
- Landry, J.W. et al. (2011) Genes Dev 25, 275-86.
- Landry, J. et al. (2008) PLoS Genet 4, e1000241.
Application References
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For Research Use Only. Not For Use In Diagnostic Procedures.