Product Pathways - Chromatin Regulation / Epigenetics
SS18 (D6I4Z) Rabbit mAb #21792
|21792S||100 µl ( 10 western blots )||￥3,250.00 现货查询||购买询价|
|21792||carrier free & custom formulation / quantity||email request|
|W||1:1000||Human,Mouse,Rat,Monkey,||Endogenous||Iso1 60, Iso2 50||Rabbit IgG|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IP=Immunoprecipitation, ChIP=Chromatin IP,
Species predicted to react based on 100% sequence homology: Dog, Horse,
Specificity / Sensitivity
SS18 (D6I4Z) Rabbit mAb recognizes endogenous levels of total SS18 protein.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gln394 of human SS18 protein.
Western blot analysis of extracts from various cell lines using SS18 (D6I4Z) Rabbit mAb.
Immunoprecipitation of SS18 from ACHN cell extracts. Lane 1 is 10% input, lane 2 is Rabbit (DA1E) mAb IgG XP® Isotype control #3900, and lane 3 is SS18 (D6I4Z) Rabbit mAb. Western blot analysis was performed using SS18 (D6I4Z) Rabbit mAb.
Chromatin immunoprecipitations were performed with cross-linked chromatin from 4 x 106 MCF7 cells grown in phenol red free medium and 5% charcoal stripped FBS for 4 d then treated with β-estradiol (10 nM) for 45 min and either 10 μl of SS18 (D6I4Z) Rabbit mAb or 2 μl of Normal Rabbit IgG #2729 using SimpleChIP® Enzymatic Chromatin IP Kit (Magnetic Beads) #9003. The enriched DNA was quantified by real-time PCR using SimpleChIP® Human ESR1 Promoter Primers #9673, SimpleChIP® Human pS2 Promoter Primers #9702, and SimpleChIP® Human α Satellite Repeat Primers #4486. The amount of immunoprecipitated DNA in each sample is represented as signal relative to the total amount of input chromatin, which is equivalent to one.
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).
SS18 is a protein that has been shown to be a part of the SWI/SNF complex (10, 11). The SS18-SSX fusion proteins are a result of in-frame fusions that fuse the SS18 gene on chromosome 18 with X chromosome genes SSX1, SSX2, and to a lesser extent SSX4 (12). Human synovial sarcoma (SS) accounts for 8-10% of all soft tissue malignancies and 95% of these malignancies express the recurrent translocation of the SS18 gene on chromosome 18 (12). The N-terminal SNH domain (SYT N-terminal homology domain) of the SS18 protein interacts with SWI/SNF chromatin remodeling complexes via the N terminal region of BRM and BRG1 subunits (13). Studies of the SS18-SSX fusion in SS suggest that endogenous SS18 competes with the mutant SS18-SSX fusion for occupancy in the SWI/SNF complexes resulting in the displacement of SNF5 (BAF47) subunit. Displacement of the SNF5 subunit results in altered function of the SWI/SNF complex that leads to deregulated expression of genes such as Sox2 in SS (12).
In addition, cytosolic SS18 isoforms also associate with F-actin in cytoskeletal organization (14). SS18 null mice do not develop beyond E9.5 and have defects in vascularization, cell migration, neural tube closure, and fusion within the embryonic-maternal membranes (14).
- 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.
- Nagai, M. et al. (2001) Proc Natl Acad Sci U S A 98, 3843-8.
- Thaete, C. et al. (1999) Hum Mol Genet 8, 585-91.
- Kadoch, C. and Crabtree, G.R. (2013) Cell 153, 71-85.
- Perani, M. et al. (2003) Oncogene 22, 8156-67.
- Kim, J. et al. (2009) PLoS One 4, e6455.
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