Anti-Asymmetric Dimethylarginine of TLS/FUS (R216, R218), Human, Mouse-mono (100 ug)

Anti-Asymmetric Dimethylarginine of TLS/FUS (R216, R218), Human, Mouse-mono


General information 

Antigen Characterization   

• Is a specific post-translational modification of TLS/FUS protein
• Involves asymmetric dimethylation of arginine residues at positions 216 and 218
• Carried out by protein arginine methyltransferases (PRMTs), particularly PRMT1
• Exact function not fully understood, but believed to:
  • Regulate TLS/FUS protein interactions
  • Influence protein localization
  • Affect involvement in RNA metabolism processes (transcription, pre-mRNA splicing, mRNA transport)
  • Potentially modify the protein's ability to bind RNA
  • Possibly impact participation in various cellular complexes

• Of particular interest in the context of neurodegenerative diseases, especially ALS
• TLS/FUS is a known causative gene for familial ALS
• Alterations in methylation patterns may contribute to ALS pathogenesis
• Specific role in healthy individuals still under research
• Likely involved in:
  • Normal functioning of neurons
  • Processes in other cells where TLS/FUS is expressed
• Understanding this modification could provide insights into:
  • Normal cellular processes
  • Mechanisms underlying neurodegenerative disorders

Aliases for TLS/FUS (R216, R218) Gene

• Fused in Sarcoma
• Translocated in Sarcoma
• 75 kDa DNA pairing protein

Description

This antibody recognizes asymmetric dimethylarginine (R216, R218) of TLS/FUS. It does not cross-reacts against symmetric dimethylarginine of TLS/FUS, and non -methylated TLS /FUS.

Arginine methylation is one posttranslational modification. Arginine can be methylated once (monomethylated arginine) or twice (dimethylated arginine). Dimethylation can be further categorized as symmetric (me2s) or asymmetric (me2a). TLS/FUS (Translocated in LipoSarcoma/Fused in Sarcoma) is known as one of the causative genes for familial amyotrophic lateral sclerosis. Specifically, it is reported that four arginine residues in TLS/FUS (R216, R218, R242, and R394) are constitutively dimethylated by protein arginine methyltransferases. However, the function of methylated TLS/FUS is still unclear. 

Application

Lane1 Recombinant GST-TLS/FUS methylated using PRMT1 in the presence of SAM (20 µM) in vitro. Lane2 Cell extract from CHO cells immunoprecipitated with rabbit polyclonal anti-TLS/FUS antibody (Bethyl Laboratories, #A300-302A). ※It is hard to detect the specific band for methylated TLS/FUS with crude lysate sample. We recommend to do immunoprecipitation using polyclonal anti-TLS/FUS antibody prior to WB.

 

Arginine methylation of TLS/FUS 

Type of arginine methylation

Reference

• Jun M, et al. Sequestration of PRMT1 and Nd1-L mRNA into ALS-linked FUS mutant R521C-positive aggregates contributes to neurite degeneration upon oxidative stress. Sci Rep. (2017) 7: 40474.
• Xiong, Dian et al. “Elevated FUS/TLS expression is negatively associated with E-cadherin expression and prognosis of patients with non-small cell lung cancer.” Oncology letters vol. 16,2 (2018): 1791-1800. doi:10.3892/ol.2018.8816
• Kino, Y., Washizu, C., Kurosawa, M. et al. FUS/TLS acts as an aggregation-dependent modifier of polyglutamine disease model mice. Sci Rep 6, 35236 (2016). https://doi.org/10.1038/srep35236
• Tan, Adelene Y, and James L Manley. “TLS/FUS: a protein in cancer and ALS.” Cell cycle (Georgetown, Tex.) vol. 11,18 (2012): 3349-50. doi:10.4161/cc.21875
• Kino, Y., Washizu, C., Kurosawa, M. et al. FUS/TLS deficiency causes behavioral and pathological abnormalities distinct from amyotrophic lateral sclerosis. acta neuropathol commun 3, 24 (2015). https://doi.org/10.1186/s40478-015-0202-6
• Ward, C., Boggio, K., Johnson, B. et al. A loss of FUS/TLS function leads to impaired cellular proliferation. Cell Death Dis 5, e1572 (2014). https://doi.org/10.1038/cddis.2014.508
• “FUS.” FUS - an Overview | ScienceDirect Topics, www.sciencedirect.com/topics/agricultural-and-biological-sciences/fus.