| Species : |
Human |
| Source : |
Human |
| Tag : |
His |
| Protein Length : |
1-105 a.a. |
| Description : |
Thioredoxins are small disulphide-containing redox proteins (within the conserved Cys-Gly-Pro-Cys active site) that have been found in all the kingdoms of living organisms. Thioredoxin contains a single disulfide active site and serves as a general protein disulphide oxidoreductase. Thioredoxins are involved in the first unique step in DNA synthesis. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. It has been suggested that thioredoxin may catalyze the formation of correct disulfides during protein folding because of its ability to act as an efficient oxidoreductant. Trx also provides control over a number of transcription factors affecting cell proliferation and death through a mechanism referred to as redox regulation. |
| Form : |
TXN1 solution containing 1x PBS pH 7.4. |
| Purity : |
Greater than 95.0% as determined by SDS-PAGE. |
| Bio-activity : |
Specific activity is 7-10 A650/min/mg, obtained by measuring the increase of insulin precipitation in absorbance at 650 nm resulting from the reduction of insulin. |
| Physical Appearance : |
Sterile filtered colorless solution. |
| Amino acid sequence : |
MGSSHHHHHH SSGLVPRGSH MVKQIESKTA FQEALDAAGD KLVVVDFSAT WCGPCKMIKP FFHSLSEKYS NVIFLEVDVD DCQDVASECE VKCMPTFQFF KKGQKVGEFS GANKEKLEAT INELV. |
| Storage : |
Thioredoxin human although stable at 4ºC for 1 week, should be stored desiccated below -18ºC. Please prevent freeze thaw cycles. |
| Pathways : |
Nucleotide metabolism |
