DTNB; Ellman's Reagent, 5,5'-Dithiobis-(2-Nitrobenzoic Acid)

DTNB; reactivo de Ellman, 5,5'-ditiobis-(2-ácido nitrobenzóico)

Número de catálogo	Cantidad
D8451	10 g

Número de catálogo D8451

Precio (MXN)

Cantidad:

DTNB or Elman's reagent can be used to quantitate thiols in proteins, cells and plasma by absorption measurements. It readily forms a mixed disulfide with thiols, liberating the chromophore 5-merapto-2-nitrobenzoic acid (absorption maximum 410 nm). Only protein thiols that are accessible to this water-soluble reagent are modified.

El reactivo de DTNB o Elman se puede utilizar para cuantificar tioles en proteínas, células y plasma mediante mediciones de absorción. Forma fácilmente un disulfuro mezclado con tioles, liberando el ácido cromóforo 5-merapto-2-nitrobenzoico (absorción máxima de 410 nm). Solo se modifican los tioles proteicos que son accesibles a este reactivo soluble en agua.

Para uso exclusivo en investigación. No apto para uso en procedimientos diagnósticos.

Especificaciones

Cantidad10 g

Tipo de productoReactivo de Elman

Unit SizeEach

Citations & References (181)

Citations & References

Abstract

Spatial proximity of Cys113, Cys172, and Cys422 in the metalloactivation domain of the ArsA ATPase.

Authors:Bhattacharjee H,Rosen BP

Journal:The Journal of biological chemistry

PubMed ID:8798705

A general strategy for site-specific double labeling of globular proteins for kinetic FRET studies.

Authors:Ratner V,Kahana E,Eichler M,Haas E

Journal:Bioconjugate chemistry

PubMed ID:12236801

Site-directed mutagenesis provides a straightforward means of creating specific targets for chemical modifications of proteins. This capability enhanced the applications of spectroscopic methods adapted for addressing specific structural questions such as the characterization of partially folded and transient intermediate structures of globular proteins. Some applications such as the steady state ... More

Reactivity of mitochondrial sulfhydryl groups toward dithionitrobenzoic acid and bromobimanes under oligomycin-inhibited and uncoupling conditions.

Authors:Freisleben HJ, Fuchs J, Mainka L, Zimmer G

Journal:Arch Biochem Biophys

PubMed ID:2845867

Thiol reactivity was determined in rat heart mitochondria using chromophores of differing polarities: monobromobimane (MB), dithionitrobenzoate (NbS2), and bromobimane-q (MQ). The purpose of this study is to correlate reaction rates of protein thiols in the mitochondrial membrane with the oligomycin-inhibited and uncoupled states: In all cases investigated the reactivity of ... More

Sulfhydryl groups of rabbit liver arylsulfatase A.

Authors:Waheed A, Van Etten RL

Journal:Biochim Biophys Acta

PubMed ID:2864083

Rabbit liver arylsulfatase A (aryl-sulfate sulfhydrolase, EC 3.1.6.1) monomers of 130 kDa contain two free sulfhydryl groups as determined by spectrophotometric titration using 5,5'-dithiobis(2-nitrobenzoate) and by labeling with the fluorescent probe 5-(iodoacetamidoethyl)aminonaphthalene-1-sulfonic acid. Fluorescence quenching data indicate that the reactive sulfhydryl is present in proximity to one or more tryptophan ... More

Actin can act as a cofactor for a viral proteinase in the cleavage of the cytoskeleton.

Authors:Brown MT, McBride KM, Baniecki ML, Reich NC, Marriott G, Mangel WF

Journal:J Biol Chem

PubMed ID:12191991

'Cytoskeletal proteins are exploited by many viruses during infection. We report a novel finding that actin can act as a cofactor for the adenovirus proteinase (AVP) in the degradation of cytoskeletal proteins. Transfection studies in HeLa cells revealed AVP localized with cytokeratin 18, and this was followed by destruction of ... More

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