Cell Signaling Technology

Product Pathways - Chromatin Regulation / Epigenetics

SMARCA1 Antibody #9450

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.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using SMARCA1 Antibody.

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).

  1. Lazzaro, M.A. and Picketts, D.J. (2001) J Neurochem 77, 1145-56.
  2. Erdel, F. and Rippe, K. (2011) FEBS J 278, 3608-18.
  3. Barak, O. et al. (2003) EMBO J 22, 6089-100.
  4. Banting, G.S. et al. (2005) Hum Mol Genet 14, 513-24.
  5. Ho, L. and Crabtree, G.R. (2010) Nature 463, 474-84.
  6. Landry, J.W. et al. (2011) Genes Dev 25, 275-86.
  7. 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.

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