Molecular structure of MTS-TEAE
MTS-TEAE
Alternate Names:
2-(Triethylammonium)ethyl Methanethiosulfonate Bromide
Application:
MTS-TEAE is water soluble, bulkier analogue of the charged MTS reagent MTSET
Purity:
≥97%
Molecular Weight:
320.30
Molecular Formula:
C9H22BrNO2S2
For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.
* Refer to Certificate of Analysis for lot specific data.
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Description
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SDS & Certificate of Analysis
MTS-TEAE is a water soluble, bulkier analogue of the charged MTS reagent MTSET. Charged MTS reagents have been used successfully with SCAM (substituted cysteine accessibility method) to probe the topology and function of a number of ligand-gated ion channels and transporter proteins. MTS-TEAE, also known as (2-(Trimethylammonium)ethyl) methanethiosulfonate, is used in bioconjugation and protein modification studies. It is a sulfhydryl-reactive reagent that selectively reacts with cysteine residues in proteins, forming a covalent bond. MTS-TEAE is often employed in site-directed mutagenesis and protein engineering techniques to introduce specific modifications or probes at cysteine residues.
MTS-TEAE References
- Structural determinants of ion permeation in CRAC channels. | McNally, BA., et al. 2009. Proc Natl Acad Sci U S A. 106: 22516-21. PMID: 20018736
- Participation of transmembrane domain 1 of presenilin 1 in the catalytic pore structure of the γ-secretase. | Takagi, S., et al. 2010. J Neurosci. 30: 15943-50. PMID: 21106832
- Cooperative roles of hydrophilic loop 1 and the C-terminus of presenilin 1 in the substrate-gating mechanism of γ-secretase. | Takagi-Niidome, S., et al. 2015. J Neurosci. 35: 2646-56. PMID: 25673856
- The STIM-Orai Pathway: Orai, the Pore-Forming Subunit of the CRAC Channel. | Gudlur, A. and Hogan, PG. 2017. Adv Exp Med Biol. 993: 39-57. PMID: 28900908
- Conformational Dynamics of Transmembrane Domain 3 of Presenilin 1 Is Associated with the Trimming Activity of γ-Secretase. | Cai, T., et al. 2019. J Neurosci. 39: 8600-8610. PMID: 31527118
- Interrogating permeation and gating of Orai channels using chemical modification of cysteine residues. | Yamashita, M. and Prakriya, M. 2021. Methods Enzymol. 652: 213-239. PMID: 34059283
- Structural Analysis of Target Protein by Substituted Cysteine Accessibility Method. | Cai, T. and Tomita, T. 2018. Bio Protoc. 8: e2470. PMID: 34395783
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
MTS-TEAE, 10 mg | sc-215395 | 10 mg | $379.00 |