Thioredoxin-1/TRXA Protein, E.coli (His)

Thioredoxin-1/TRXA Protein participates in diverse redox reactions, facilitating reversible oxidation of its active center dithiol to form a disulfide bond and catalyzing critical dithiol-disulfide exchanges. Operating as a monomer, Thioredoxin-1 exhibits versatility in redox functions and interacts with bacteriophage T3 DNA polymerase, suggesting broader involvement in molecular processes beyond its primary redox activities. Thioredoxin-1/TRXA Protein, E.coli (His) is the recombinant E. coli-derived Thioredoxin-1/TRXA protein, expressed by E. coli , with N-His labeled tag. The total length of Thioredoxin-1/TRXA Protein, E.coli (His) is 108 a.a., with molecular weight of ~15.7 kDa.

Thioredoxin-1/TRXA Protein actively engages in diverse redox reactions by facilitating the reversible oxidation of its active center dithiol to form a disulfide bond, and it catalyzes critical dithiol-disulfide exchange reactions. Operating as a monomer, Thioredoxin-1 demonstrates versatility in its redox functions. Notably, it interacts with bacteriophage T3 DNA polymerase, suggesting its involvement in molecular processes beyond its primary redox activities.

E.coli

E. coli

N-His

P0AA25 (2S-109A)

69484444  [NCBI]

SDKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGEVAATKVGALSKGQLKEFLDANLA

Approximately 15.7 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.