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1,2-Ethanediyl Bismethanethiosulfonate (CAS 55-95-8)

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Alternate Names:
1,2-Ethanedithiol Dimethanesulfonate; Preparation 289; MTS-2-MTS
Application:
1,2-Ethanediyl Bismethanethiosulfonate is a homobifunctional sulfhydryl-reactive crosslinker, 4 atom spacer arm
CAS Number:
55-95-8
Molecular Weight:
250.36
Molecular Formula:
C4H10O4S4
For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.
* Refer to Certificate of Analysis for lot specific data.

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1,2-Ethanediyl bismethanethiosulfonate is a chemical compound utilized in the study of protein folding and structure. This compound serves as a crosslinker for cysteine residues in peptides and proteins, enabling researchers to stabilize protein-protein interactions and to investigate quaternary structures under non-denaturing conditions. By facilitating the formation of disulfide bonds between cysteine residues, 1,2-ethanediyl bismethanethiosulfonate is instrumental in elucidating the spatial arrangement of protein complexes. Its role in the analysis of protein conformational changes is critical for understanding the dynamics of protein function. Furthermore, this compound is used in the exploration of redox processes within proteins, contributing to a deeper understanding of cellular signaling pathways and redox regulation.


1,2-Ethanediyl Bismethanethiosulfonate (CAS 55-95-8) References

  1. Determining the dimensions of the drug-binding domain of human P-glycoprotein using thiol cross-linking compounds as molecular rulers.  |  Loo, TW. and Clarke, DM. 2001. J Biol Chem. 276: 36877-80. PMID: 11518701
  2. Vanadate trapping of nucleotide at the ATP-binding sites of human multidrug resistance P-glycoprotein exposes different residues to the drug-binding site.  |  Loo, TW. and Clarke, DM. 2002. Proc Natl Acad Sci U S A. 99: 3511-6. PMID: 11891276
  3. Unraveling functional and structural interactions between transmembrane domains IV and XI of NhaA Na+/H+ antiporter of Escherichia coli.  |  Galili, L., et al. 2004. J Biol Chem. 279: 23104-13. PMID: 15039449
  4. Contribution of presenilin transmembrane domains 6 and 7 to a water-containing cavity in the gamma-secretase complex.  |  Tolia, A., et al. 2006. J Biol Chem. 281: 27633-42. PMID: 16844686
  5. Monomers of the NhaA Na+/H+ antiporter of Escherichia coli are fully functional yet dimers are beneficial under extreme stress conditions at alkaline pH in the presence of Na+ or Li+.  |  Rimon, A., et al. 2007. J Biol Chem. 282: 26810-26821. PMID: 17635927
  6. Inter-subunit disulfide cross-linking in homomeric and heteromeric P2X receptors.  |  Marquez-Klaka, B., et al. 2009. Eur Biophys J. 38: 329-38. PMID: 18427801
  7. Mapping of interdomain interfaces required for the functional architecture of Yor1p, a eukaryotic ATP-binding cassette (ABC) transporter.  |  Pagant, S., et al. 2008. J Biol Chem. 283: 26444-51. PMID: 18644782
  8. Movements of native C505 during channel gating in CNGA1 channels.  |  Nair, AV., et al. 2009. Eur Biophys J. 38: 465-78. PMID: 19132361
  9. Conformational rearrangements in the S6 domain and C-linker during gating in CNGA1 channels.  |  Nair, AV., et al. 2009. Eur Biophys J. 38: 993-1002. PMID: 19488745
  10. Conformational plasticity of the type I maltose ABC importer.  |  Böhm, S., et al. 2013. Proc Natl Acad Sci U S A. 110: 5492-7. PMID: 23509285
  11. Two salt bridges differentially contribute to the maintenance of cystic fibrosis transmembrane conductance regulator (CFTR) channel function.  |  Cui, G., et al. 2013. J Biol Chem. 288: 20758-67. PMID: 23709221
  12. Probing the proton channels in subunit N of Complex I from Escherichia coli through intra-subunit cross-linking.  |  Tursun, A., et al. 2016. Biochim Biophys Acta. 1857: 1840-1848. PMID: 27632419
  13. Mechanistic insights into the regulation of plant phosphate homeostasis by the rice SPX2 - PHR2 complex.  |  Guan, Z., et al. 2022. Nat Commun. 13: 1581. PMID: 35332155

Ordering Information

Product NameCatalog #UNITPriceQtyFAVORITES

1,2-Ethanediyl Bismethanethiosulfonate, 25 mg

sc-208746
25 mg
$403.00