TPE-MI

For research use only. Not for therapeutic Use.

  • CAT Number: I045198
  • CAS Number: 1245606-71-6
  • Molecular Formula: C31H23NO2
  • Molecular Weight: 441.52
  • Purity: ≥95%
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TPE-MI (Tetraphenylethene maleimide) is a thiol probe for measuring unfolded protein load and proteostasis in cells. TPE-MI can report imbalances in proteostasis in induced pluripotent stem cell models of Huntington disease, as well as cells transfected with mutant Huntington exon 1 before the formation of visible aggregates. TPE-MI also detects protein damage following dihydroartemisinin research of the malaria parasitesPlasmodium falciparum [1][2].
TPE-MI is inherently non-fluorescent until it is conjugated to a thiol via the maleimide. TPE-MI fluorescence is activated upon labelling free cysteine thiols, normally buried in the core of globular proteins that are exposed upon unfolding[1].
TPE-MI (50 μM; 0-60 min) exhibits a homogeneous cytoplasmic labelling pattern in live HeLa cells, with a lower level of labelling in the nucleus and apparent concentration in the region of the ER, which was anticipated as a major location for protein synthesis and folding[1].
At the high expression level, the mutant 97Q form of Httex1 was associated with an elevated TPE-MI fluorescence signal relative to a non-disease-causing 25Q form of Httex1[1].
TPE-MI consists of the aggregation-induced emission (AIE) fluorogen tetraphenylethane (TPE) and the thiol-reactive group maleimide (MI), thereby possessing both AIE phenomenon and selective thiol reactivity[2].


Catalog Number I045198
CAS Number 1245606-71-6
Synonyms

1-[4-[(Z)-2-(4-methylphenyl)-1,2-diphenylethenyl]phenyl]pyrrole-2,5-dione

Molecular Formula C31H23NO2
Purity ≥95%
InChI InChI=1S/C31H23NO2/c1-22-12-14-25(15-13-22)30(23-8-4-2-5-9-23)31(24-10-6-3-7-11-24)26-16-18-27(19-17-26)32-28(33)20-21-29(32)34/h2-21H,1H3/b31-30-
InChIKey CIMVFJJQFXGASK-KTMFPKCZSA-N
SMILES CC1=CC=C(C=C1)C(=C(C2=CC=CC=C2)C3=CC=C(C=C3)N4C(=O)C=CC4=O)C5=CC=CC=C5
Reference

[1]. Chen MZ, et al. A thiol probe for measuring unfolded protein load and proteostasis in cells. Nat Commun. 2017;8(1):474. Published 2017 Sep 7.
 [Content Brief]

[2]. Hu Q, et al. In Situ Monitored Vortex Fluidic-Mediated Protein Refolding/Unfolding Using an Aggregation-Induced Emission Bioprobe. Molecules. 2021;26(14):4273. Published 2021 Jul 14.
 [Content Brief]

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