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Thiol-specific spin label
Highly reactive thiol-specific spin label. Has been 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.
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Product Details
| Alternative Name |
(1-Oxyl-2,2,5,5-tetramethylpyrroline-3-methyl) methanethiosulfonate |
|---|---|
| Appearance |
Yellow crystalline solid. |
| CAS |
81213-52-7 |
| Formula |
C10H18NO3S2 |
| MW |
264.3 |
| Purity |
≥98% (HPLC) |
| Solubility |
Soluble in water, methanol, 100% ethanol, DMSO, acetonitrile or acetone. |
Handling & Storage
| Use/Stability |
As indicated on product label or CoA when stored as recommended. |
|---|---|
| Handling |
Protect from light. |
| Long Term Storage |
-20°C |
| Shipping |
Blue Ice |
| Regulatory Status |
RUO – Research Use Only |
|---|
- Cholesterol twists the transmembrane Di-Gly region of amyloid-precursor protein: D.T. Wang, et al.; PNAS Nexus 2, pgad162 (2023), Abstract — Full Text
- Structural Insights into the Binding and Degradation Mechanisms of Protoporphyrin IX by the Translocator Protein TSPO: P.S. Yeh, et al.; JACS Au 3, 2918 (2023), Abstract
- Rapid Scan Electron Paramagnetic Resonance Spectroscopy Is a Suitable Tool to Study Intermolecular Interactions of Intrinsically Disordered Protein: J. Dröden, et al.; Biology 12, 79 (2023), Abstract
- Structure and mechanism of human cystine exporter cystinosin: X. Guo, et al.; Cell 185, 3739 (2022), Abstract
- Nanodisc Lipids Exhibit Singular Behaviors Implying Critical Phenomena: P.S. Ho, et al.; Langmuir 49, 15372 (2022), Abstract
- Proton-driven alternating access in a spinster lipid transporter: R. Dastvan, et al.; Nat. Commun. 13, 5161 (2022), Abstract
- Location of the cross-β structure in prion fibrils: A search by seeding and electron spin resonance spectroscopy: B.K.Y. Chu, et al.; Protein Sci. 31, e4326 (2022), Abstract
- Protein and solutes freeze-concentration in water/glycerol mixtures revealed by pulse EPR: N. Isaev, et al.; Eur. J. Pharm. Biopharm. 169, 44 (2021), Abstract
- A molecular switch regulating transcriptional repression and activation of PPARγ: Shang, J., Mosure, S. A., et al.; Nat. Commun. 11, 956 (2020), Abstract
- Conformational transitions of the sodium-dependent sugar transporter, vSGLT: A. Paz, et al.; PNAS 115, E2742 (2018), Abstract — Full Text
- Lipids modulate the conformational dynamics of a secondary multidrug transporter: C. Martens, et al.; Nat. Struct. Mol. Biol. 23, 744 (2016), Application(s): Spin-labeling, after LmrP mutant purification, Abstract
- A new structural model of Alzheimer’s Aβ42 fibrils based on electron paramagnetic resonance data and Rosetta modeling: L. Gu, et al.; J. Struct. Biol. 194, 61 (2016), Application(s): Cell culture, Abstract
- Protonation-dependent conformational dynamics of the multidrug transporter EmrE: R. Dastvan, et al.; PNAS 113, 1220 (2016), Abstract — Full Text
- Conformational dynamics of the nucleotide binding domains and the power stroke of a heterodimeric ABC transporter: S. Mishra et al.; eLife 3, e02740 (2014), Application(s): Size-exclusion chromatography, Abstract — Full Text
- The Structure of the RLIP76 RhoGAP-Ral Binding Domain Dyad: Fixed Position of the Domains Leads to Dual Engagement of Small G Proteins at the Membrane: K.V. Rajasekar, et al.; Structure 21, 2131 (2013), Application(s): Mass spectrometry, Assay, Abstract — Full Text
- Alzheimer’s Aβ42 and Aβ40 peptides form interlaced amyloid fibrils: L. Gu, et al.; J. Neurochem. 126, 305 (2013), Application(s): MALDI-TOF mass spectrometry, Abstract — Full Text
- Hierarchical Organization in the Amyloid Core of Yeast Prion Protein Ure2: S. Ngo, et al.; J. Biol. Chem. 286, 29691 (2011), Application(s): MALDI-TOF mass spectrometry, Abstract — Full Text
- Calcium structural transition of human cardiac troponin C in reconstituted muscle fibres as studied by site-directed spin labelling: M. Nakamura, et al.; J. Mol. Biol. 348, 127 (2005), Abstract
- 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), Abstract
- Spontaneous refolding of the pore-forming Colicin A toxin upon membrane association as studied by X-band and W-band high-field electron paramagnetic resonance spectroscopy: A. Savitski, et al.; J. Phys. Chem. B 108, 9541 (2004)
- 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), Abstract
- 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), Abstract
- Pressure-induced thermostabilization of glutamate dehydrogenase from the hyperthermophile Pyrococcus furiosus: M.M. Sun, et al.; Protein Sci. 8, 1056 (1999), Abstract
- A novel reversible thiol-specific spin label: papain active site labeling and inhibition: L.J. Berliner, et al.; Anal. Biochem. 119, 450 (1982), Abstract
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SDS
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