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45245

Eosin 5-isothiocyanate

≥95.0% (UV)

Synonym(s):

EITC

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About This Item

Empirical Formula (Hill Notation):
C21H7Br4NO5S
CAS Number:
Molecular Weight:
704.96
UNSPSC Code:
12352200
PubChem Substance ID:
MDL number:


assay

≥95.0% (UV)

fluorescence

λex 521; λem 544 (pH 9.0)

storage temp.

2-8°C

SMILES string

OC(=O)c1cc(ccc1C2=C3C=C(Br)C(=O)C(Br)=C3Oc4c(Br)c(O)c(Br)cc24)N=C=S

InChI

1S/C21H7Br4NO5S/c22-12-4-10-14(8-2-1-7(26-6-32)3-9(8)21(29)30)11-5-13(23)18(28)16(25)20(11)31-19(10)15(24)17(12)27/h1-5,27H,(H,29,30)

InChI key

MCXYFYWNOWPDMA-UHFFFAOYSA-N

Application

Eosin 5-isothiocyanate (EITC) is a fluorescence probe. EITC tagged molecules may be used together with fluorescein-5′-isothiocyanate (FITC) tagged molecules in fluoresce resonance energy transfer (FRET) based assays.

Other Notes

Acceptor fluorophore. Measurement of rotational diffusion of proteins; In fluorescence energy transfer studies[1][2]


pictograms

Health hazard

signalword

Danger

Hazard Classifications

Resp. Sens. 1 - Skin Sens. 1

Storage Class

13 - Non Combustible Solids

wgk

WGK 3

flash_point_c

Not applicable

ppe

dust mask type N95 (US), Eyeshields, Faceshields, Gloves

flash_point_f

Not applicable

hcodes



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Articles

Nitric oxide (NO) as a signal transporter in neurons, endothelial cells and in the immune system.


T Chiba et al.
Biochimica et biophysica acta, 897(1), 14-24 (1987-02-12)
The characteristics of the anion transport system in human erythrocyte, which can be modified by eosin 5-isothiocyanate (EITC), were studied using the pH titration method and by measuring the sulfate efflux. Based on the pH dependence of EITC binding to
S Q Liu et al.
The American journal of physiology, 264(5 Pt 1), C1155-C1164 (1993-05-01)
Although eosin-5-maleimide (EM) covalently labels band 3 and has been thought to react at the external-facing anion transport site, EM reversibly inhibits Cl- exchange at 0 degrees C in a noncompetitive fashion, indicating that under these conditions it does not
Valeria Levi et al.
Biochimica et biophysica acta, 1599(1-2), 141-148 (2002-12-14)
Self-association of bovine serum albumin (BSA) was explored using fluorescence resonance energy transfer (FRET) between two populations of the protein labeled separately with either fluorescein-5'-isothiocyanate (FITC) or eosin-5'-isothiocyanate (EITC). The energy transfer reached the steady state after 5 s at



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