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Key Documents

T0803

Sigma-Aldrich

Anti-Thioredoxin antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

Sinonimo/i:

Anti-Thioredoxin

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About This Item

Codice UNSPSC:
12352203
NACRES:
NA.46

Origine biologica

rabbit

Livello qualitativo

Coniugato

unconjugated

Forma dell’anticorpo

IgG fraction of antiserum

Tipo di anticorpo

primary antibodies

Clone

polyclonal

Forma fisica

buffered aqueous solution

Confezionamento

antibody small pack of 25 μL

tecniche

dot blot: 1:5,000 using purified recombinant thioredoxin
western blot: 1:5,000 using E. coli extract

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

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Descrizione generale

The thioredoxin system consists of thioredoxin, thioredoxin-reductase and NADPH. Thioredoxin from E. coli consists of a single polypeptide chain of 108 amino acids with a molecular weight of 11,700. The protein contains no prosthetic group or bound metals.

Specificità

Specific for natural E. coli and recombinant thioredoxin. It may be used to identify and purify the expression of thioredoxin fusion proteins.

Immunogeno

recombinant E. coli thioredoxin.

Applicazioni

Anti-Thioredoxin antibody produced in rabbit has been used in:
  • immunohistochemistry
  • immunoblotting
  • dot blot immunoassay
  • ouchterlony double diffusion
  • immunodetection
  • western blotting

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunohistochemistry (1 paper)
Immunofluorescence was carried out on the cerivcal cancer cell lines SiHa, CaSki, and HeLa using an antibody against the redox proteinThioredoxin.

Azioni biochim/fisiol

Thioredoxin is a small electron transport protein that serves as the hydrogen donor in the enzymatic reduction of ribonucleotides to deoxyribonucleotides. The thioredoxin system is involved in other reductive processes such as the enzymatic reduction of methionine sulfoxide and sulfate. The oxidation-reduction function of thioredoxin is linked to a single intra-molecular disulfide bridge, forming a 14 member ring. The system is particularly useful for high level production of soluble fusion proteins in the E. coli cytoplasm. In many cases, these fusion proteins fold correctly and thus display full biological activity.

Stato fisico

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Esclusione di responsabilità

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

nwg

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Certificati d'analisi (COA)

Cerca il Certificati d'analisi (COA) digitando il numero di lotto/batch corrispondente. I numeri di lotto o di batch sono stampati sull'etichetta dei prodotti dopo la parola ‘Lotto’ o ‘Batch’.

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Thioredoxin and thioredoxin target proteins: from molecular mechanisms to functional significance
Lee S, et al.
Antioxidants & Redox Signaling, 18(10), 1165-1207 (2013)
Fusion tags for protein solubility, purification and immunogenicity in Escherichia coli: the novel Fh8 system
Costa S, et al.
Frontiers in Microbiology, 5(22), 63-63 (2014)
Thioredoxin 1 participates in the activity of the Salmonella enterica serovar Typhimurium pathogenicity island 2 type III secretion system
Negrea A, et al.
Journal of Bacteriology, 191(22), 6918-6927 (2009)
N Vázquez-Laslop et al.
Journal of bacteriology, 183(8), 2399-2404 (2001-03-29)
Escherichia coli cells, the outer membrane of which is permeabilized with EDTA, release a specific subset of cytoplasmic proteins upon a sudden drop in osmolarity in the surrounding medium. This subset includes EF-Tu, thioredoxin, and DnaK among other proteins, and
The anti-tumor effects of calorie restriction are correlated with reduced oxidative stress in ENU-induced gliomas
Mahlke MA, et al
Pathobiology of aging & age related diseases, 1(1), 7189-7189 (2011)

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