| ADI-SPP-892-200 | 200 µg | 269.00 USD |  |
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| ADI-SPP-892-1 | 1 mg | 714.00 USD | |
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| Alternative Name: | Trx |
| Recommended Dilutions/Conditions: | Activity Assay (>300U/mg) Western Blot (100ng, colorimetric) Suggested dilutions/conditions may not be available for all applications. Optimal conditions must be determined individually for each application. |
| MW: | ~12kDa |
| Source: | Produced in E. coli. E. coli thioredoxin is fused at the N-terminus to a His-tag. |
| Formulation: | Liquid. In 50mM TRIS, pH 7.5, containing 100mM sodium chloride and 1mM EDTA. |
| Purity: | ≥95% (SDS-PAGE; Western blot) |
| Purity Detail: | Purified by multi-step chromatography. |
| Applications: | WB Activity assay |
| Application Notes: | Western blot control. |
| Shipping: | Shipped on Dry Ice |
| Long Term Storage: | -80°C |
| Scientific Background: | Thioredoxin (Trx) is a redox protein of approximately 12 kDa. Its primary domain is conserved across a number of Trx family members and contains a conserved catalytic site Cys-Gly-Pro-Cys. It is ubiquitous and found in many organisms from bacteria to mammals. Trx has been shown to function in cell proliferation, redox signaling and inhibition of apoptosis. Trx is reduced by the NADPH-dependent flavoenzyme thioredoxin reductase, and in turn reduces other proteins such as protein disulfide isomerase (PDI) by cysteine thiol-disulfide exchange. Trx has been reported to selectively activate the DNA binding of a number of transcription factors such as p53, NFkB, AP1 and glucocorticoid receptor, resulting in alteration of gene transcription. The reduced Trx can supply reducing equivalents for ribonucleotide reductase, the essential enzyme for DNA synthesis, and thioredoxin peroxidase. As a cofactor for the peroxiredoxins, Trx plays a direct role in reducing oxidative species such as H2O2. |
| Regulatory Status: | RUO - Research Use Only |
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