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045050 MTSSL CAS: 81213-52-7

Specifications
References
CAS Number
81213-52-7
Grade
Highly Purified
Molecular Formula
C10H18NO3S2
Molecular Weight
264.3
EU Commodity Code
38220090
Shipping Temp
RT
Storage Temp
-20°C

Highly reactive, thiol-specific spin-label. Specific conformational probe of thiol site structure by its minimal rotational freedom and distance from the covalent disulfide linkage to the macromolecule under study. Used to label cysteine residues in proteins (site-directed labeling, SDS-labeling). Allows protein structure and protein dynamics determination as well as the study of protein-protein and protein-oligonucleotide interactions.

Synonyms
Mts-SL; MTSL; (1-Oxyl-2,2,5,5-tetramethylpyrroline-3- methyl)methanethiosulfonate; Otmpmms
CAS Number
81213-52-7
Molecular Weight
264.3
Molecular Formula
C10H18NO3S2
Solubility
Ethanol, methanol, DMSO, acetonitrile or acetone. MTSSL can be used in aqueous solution at concentrations as high as 10mM. However, MTSSL initially must be dissolved in an organic solvent such as DMSO or acetonitrile (100mM or higher) and then the initial stock solution can be diluted 10-100 fold in water-based buffers. Sonication and heating is not recommended to dissolve MTSSL.
Appearance
Supplied as a yellow crystalline solid.
Purity
≥98% (HPLC)
Storage and Stability
Store at 4°C for short term only. Protect from light. Stable for 12 months after receipt when stored at -20°C. For maximum recovery of product, centrifuge the original vial prior to removing the cap.
Important Note
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.
Toxicity and Hazards
 All products should be handled by qualified personnel only, trained in laboratory procedures.
References
1. A novel reversible thiol-specific spin label: papain active site labeling and inhibition: L.J. Berliner, et al.; Anal. Biochem. 119, 450 (1982)|2. ESR spectra reflect local and global mobility in a short spin-labeled peptide throughout the alpha-helix-coil transition: A.P. Todd & G.L. Millhauser; Biochemistry 30, 5515 (1991)|3. Kinetics and motional dynamics of spin-labeled yeast iso-1-cytochrome c: 1. Stopped-flow electron paramagnetic resonance as a probe for protein folding/unfolding of the C-terminal helix spin-labeled at cysteine 102: K. Qu, et al.; Biochemistry 36, 2884 (1997)|4. Pressure-induced thermostabilization of glutamate dehydrogenase from the hyperthermophile Pyrococcus furiosus: M.M. Sun, et al.; Protein Sci. 8, 1056 (1999)|5. Protein global fold determination using site-directed spin and isotope labeling: V. Gaponenko, et al.; Protein Sci. 9, 302 (2000)|6. High-resolution probing of local conformational changes in proteins by the use of multiple labeling: unfolding and self-assembly of human carbonic anhydrase II monitored by spin, fluorescent, and chemical reactivity probes: P. Hammarstroem, et al.; Biophys. J. 80, 2867 (2001)|7. Protein structure determination using long-distance constraints from double-quantum coherence ESR: study of T4 lysozyme: P.P. Borbat, et al.; JACS 124, 5304 (2002)|8. Methods for study of protein dynamics and protein-protein interaction in protein-ubiquitination by electron paramagnetic resonance spectroscopy: H.J. Steinhoff; Front. Biosci. 7, c97 (2002)|9. Inter- and intra-molecular distances determined by EPR spectroscopy and site-directed spin labeling reveal protein-protein and protein-oligonucleotide interaction: H.J. Steinhoff; Biol. Chem. 385, 913 (2004)|10. Dynamics of the nitroxide side chain in spin-labeled proteins: F. Tombolato, et al.; J. Phys. Chem. B. 110, 26248 (2006)|11. Parametrization, molecular dynamics simulation, and calculation of electron spin resonance spectra of a nitroxide spin label on a polyalanine alpha-helix: D. Sezer, et al.; J. Phys. Chem. B. 112, 5755 (2008)|12. Potential artifacts in using a glutathione S-transferase fusion protein system and spin labeling electron paramagnetic resonance methods to study protein-protein interactions: C. Antoniou & L.W. Fung; Anal. Biochem. 376, 160 (2008)
USBio References
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