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T0803

Sigma-Aldrich

Anti-Thioredoxin antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

Synonym(s):

Anti-Thioredoxin

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.46

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

packaging

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

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

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General description

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.

Specificity

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

Immunogen

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.

Biochem/physiol Actions

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.

Physical form

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

Disclaimer

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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Storage Class Code

10 - Combustible liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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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