351923
Clone Type
MonoclonalHost
RabbitSource
HumanIsotype
IgGClone Number
D6I4ZGrade
PurifiedApplications
ChIP IP WBCrossreactivity
Hu Mk Mo RtGene ID
6760Shipping Temp
Blue IceStorage Temp
-20°CRabbit Anti-SS18 (SSXT, SYT, Protein SSXT, Protein SYT, Synovial Sarcoma Translocated to X Chromosome 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).
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).
Applications
Suitable for use in Western Blot, Immunoprecipitation and ChIP. Other applications not tested.
Recommended Dilution
Western Blot: 1:1000, incubate membrane with diluted primary antibody in 5% BSA, 1X TBS, 0.1% Tween-20 at 4°C with gentle shaking, overnight. Immunoprecipitation: 1:50 ChIP: 1:50 Optimal dilutions to be determined by the researcher.
Storage and Stability
May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Immunogen
Synthetic peptide corresponding to residues surrounding Gln394 of human SS18. Species sequence homology: canine and equine
Form
Supplied as a liquid in 10mM sodium HEPES, pH 7.5, 0.1mg/ml BSA, 150mM sodium chloride, 0.02% sodium azide, 50% glycerol.
Specificity
Recognizes human SS18. Species Crossreactivity: mouse, monkey and rat
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
References
1. Ho, L. and Crabtree, G.R. (2010) Nature 463, 474-84. 2. Becker, P.B. and Horz, W. (2002) Annu Rev Biochem 71,247-73. 3. Eberharter, A. and Becker, P.B. (2004) J Cell Sci 117, 3707-11. 4. Bowman, G.D. (2010) Curr Opin Struct Biol 20, 73-81. 5. Gangaraju, V.K. and Bartholomew, B. (2007) Mutat Res 618,|3-17. 6. Lessard, J.A. and Crabtree, G.R. (2010) Annu Rev Cell Dev Biol 26, 503-32. 7. Morettini, S. et al. (2008) Front Biosci 13, 5522-32. 8. Wolf, I.M. et al. (2008) J Cell Biochem 104, 1580-6. 9. Simone, C. (2006) J Cell Physiol 207, 309-14. 10. Nagai, M. et al. (2001) Proc Natl Acad Sci U S A 98, 3843-8. 11. Thaete, C. et al. (1999) Hum Mol Genet 8, 585-91. 12. Kadoch, C. and Crabtree, G.R. (2013) Cell 153, 71-85. 13. Perani, M. et al. (2003) Oncogene 22, 8156-67. 14. Kim, J. et al. (2009) PLoS One 4, e6455.USBio References
No references available