| Cat. No. : |
TRX-262 |
| Description : |
Thioredoxins are small disulphide-containing redox proteins 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. 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. This could be especially useful in refolding proteins expressed in E. coli. To this end, thioredoxin has been shown to act as a protein disulfide isomerase. |
| Source : |
Recombinant E.Coli Thioredoxin was purified from E. coli harboring its gene. |
| Amino Acid Sequence : |
HMSDKIIHL TDDSFDTDVLKADGAIL VDFW AEWCGPCKMIAPILDEI GKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGEVAATKVGAL DANLA. |
| Physical Appearance : |
Sterile Lyophilized Powder. |
| Formulation : |
Each mg of protein contains 20mM phosphate buffer pH 7.4. |
| Purity : |
Greater than 90.0% as determined by: (a) Analysis by RP-HPLC. (b) Analysis by reducing and non-reducing SDS-PAGE. |
| Endotoxin : |
Less than 0.1 ng/µg (IEU/µg) of rTRX. |
| Biological Activity : |
rTRX activity is assayed by measuring the change in absorbance at 650 nm at 25°C using 0.13µM bovine insulin containing 0.33mM DTT (pH 6.5). The specific activity was found to be 3IU/mg. |
| Stability : |
rTRX although stable at 4°C for 3 weeks, should be stored desiccated below -18°C. Please prevent freeze thaw cycles. |
| Synonyms : |
TXN; MGC61975; TRX; ADF; DKFZp686B1993; MGC61975; OTTHUMP00000021892; SASP; TRDX; TRX1; Trx; thioredoxin; ATL-derived factor; Surface-associated sulphydryl protein. |
