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T0803

Sigma-Aldrich

Anti-Thioredoxin antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

Synonyme(s) :

Anti-Thioredoxin

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.46

Source biologique

rabbit

Niveau de qualité

200

Conjugué

unconjugated

Forme d'anticorps

IgG fraction of antiserum

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Conditionnement

antibody small pack of 25 μL

Technique(s)

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

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

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Description générale

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.

Spécificité

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

Immunogène

recombinant E. coli thioredoxin.

Application

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.

Actions biochimiques/physiologiques

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.

Forme physique

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

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

nwg

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

Wouter S P Jong et al.
Microbial cell factories, 16(1), 50-50 (2017-03-23)
Heterologous protein production in Escherichia coli often suffers from bottlenecks such as proteolytic degradation, complex purification procedures and toxicity towards the expression host. Production of proteins in an insoluble form in inclusion bodies (IBs) can alleviate these problems. Unfortunately, the
Chickpea ferritin CaFer1 participates in oxidative stress response, and promotes growth and development
Chakraborty S, et al.
Scientific Reports (2016)
p23 protects the human aryl hydrocarbon receptor from degradation via a heat shock protein 90-independent mechanism
Pappas B, et al.
Biochemical Pharmacology, 152(1), 34-44 (2018)
Thioredoxin 1 promotes intracellular replication and virulence of Salmonella enterica serovar Typhimurium
Bjur E, et al.
Infection and Immunity, 74(9), 5140-5151 (2006)
Mohammed Jamshad et al.
eLife, 8 (2019-06-28)
In bacteria, the translocation of proteins across the cytoplasmic membrane by the Sec machinery requires the ATPase SecA. SecA binds ribosomes and recognises nascent substrate proteins, but the molecular mechanism of nascent substrate recognition is unknown. We investigated the role
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