Thioredoxin [2B1]

2B1

Recombinant full length protein (Human).

Human Thioredoxin

Cytoplasmic

PBS pH 7. 4 with 0. 09% sodium azide as preservative.

12 kD Thioredoxin was found in yeast plants mammals and bacteria. It is a protein with two redox-active half-cystine residues in exposed active center having the following

Participates as a hydrogen donor in redox reactions through the reversible oxidation of its active center dithiol to a disulfide accompanied by the transfer of 2 electrons and 2 protons. It is involved in many cellular processes including deoxyribonucleotide synthesis repair of oxidatively damaged proteins protein folding sulfur metabolism and redox homeostasis. Thioredoxin-dependent enzymes include phosphoadenosine-phosphosulfate reductase MET16 alkyl-hydroperoxide reductase DOT5 thioredoxin peroxidases TSA1 and TSA2 alkyl hydroperoxide reductase AHP1 and peroxiredoxin HYR1. Thioredoxin is also involved in protection against reducing stress. As part of the LMA1 complex it is involved in the facilitation of vesicle fusion such as homotypic vacuole and ER-derived COPII vesicle fusion with the Golgi. This activity does not require the redox mechanism.

Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein. Nucleus.

Present with 8579 molecules/cell in log phase SD medium.

Belongs to the thioredoxin family.