T0803
Anti-Thioredoxin antibody produced in rabbit
IgG fraction of antiserum, buffered aqueous solution
Synonym(s):
Anti-Thioredoxin
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About This Item
NACRES:
NA.46
UNSPSC Code:
12352203
Conjugate:
unconjugated
Clone:
polyclonal
Application:
DB, WB
Citations:
20
biological source
rabbit
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
Quality Level
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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.
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)
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
Specific for natural E. coli and recombinant thioredoxin. It may be used to identify and purify the expression of thioredoxin fusion proteins.
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
10 - Combustible liquids
wgk
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
常规特殊物品
低风险生物材料
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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
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
The thioredoxin system in cancer
Arner ESJ and Holmgren A
Seminars in Cancer Biology, 16(6), 420-426 (2006)
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)
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Instructions
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