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.
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
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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