Thioredoxin, Recombinant, Yeast, TRX2

In S. cerevisiae three isoforms (yTRX1, yTRX2, yTRX3) have been identified, yTRX1 and yTRX2 being present in cytoplasm and yTRX3 present in mitochondria. Recombinant yTRX2 is produced by DNA recombinant procedure in E. coli as an intracellular protein and purified from cell lysate by conventional chromatographies.\n\nApplication: \nSuitable for use as an antioxidant and mitigation of allergenicity of allergic proteins in food. \n\nStorage and Stability:\nAliquot to avoid repeated freezing and thawing and store at -70 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Aliquots are stable for at least 6 months.

Prices direct from United States Biological

Quick response times

Exclusive Biosave savings/discounts

SPECIFICATIONS

Catalog Number

T5010-14C

Size

1mg

Form

Supplied as lyophilized powder.

Purity

Purified from cell lysate by conventional chromatographies.

References

1. Insertion of transposon Tn5tac1 in the Sinorhizobium meliloti malate dehydrogenase (mdh) gene results in conditional polar effects on downstream TCA cycle genes. Dymov SI, Meek DJ, Driscoll BT, Mol Plant Microbe Interact 2004 Dec;17(12):1318-27 \n2. Degradation of the gluconeogenic enzymes fructose-1,6-bisphosphatase and malate dehydrogenase is mediated by distinct proteolytic pathways and signaling events. Hung GC, Brown CR, Liu J, J Biol Chem 2004 Nov 19;279(47):49138-50 \n3. Large improvement in the thermal stability of a tetrameric malate dehydrogenase by single point mutations at the dimer-dimer interface. Bjork A, Dalhus B, Sirevag R, J Mol Biol 2004 Aug 27;341(5):1215-26 \n4. An alpha-proteobacterial type malate dehydrogenase may complement LDH function in Plasmodium falciparum. Cloning and biochemical characterization of the enzyme. Tripathi AK, Desai PV, Khan SI, Eur J Biochem 2004 Sep;271(17):3488-502 \n5. Mitochondrial malate dehydrogenase from the thermophilic, filamentous fungus Talaromyces emersonii. Maloney AP, Callan SM, Tuohy MG, Eur J Biochem 2004 Aug;271(15):3115-26 \n6. Molecular adaptation: the malate dehydrogenase from the extreme halophilic bacterium Salinibacter ruber behaves like a non-halophilic protein. Madern D, Zaccai G, Biochimie 2004 Apr-May;86(4-5):295-303.