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Thiol-specific spin label
ALX-430-134-M010 10 mg 81.00 USD
ALX-430-134-M050 50 mg 322.00 USD
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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.

Product Specification

Alternative Name:(1-Oxyl-2,2,5,5-tetramethylpyrroline-3-methyl) methanethiosulfonate
Purity:≥98% (HPLC)
Appearance:Yellow crystalline solid.
Solubility:Soluble in water, methanol, 100% ethanol, DMSO, acetonitrile or acetone.
Shipping:Shipped on Blue Ice
Long Term Storage:-20°C
Handling:Protect from light.
Regulatory Status:RUO - Research Use Only
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Product Literature References

Conformational transitions of the sodium-dependent sugar transporter, vSGLT: A. Paz, et al.; PNAS 115, E2742 (2018), Abstract; Full Text
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;
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;
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
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
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
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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