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.

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-6*His

P0AA25 (S2-A109)

69484444  [NCBI]

Full Length of Mature Protein

SDKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGEVAATKVGALSKGQLKEFLDANLA

Approximately 16 kDa, based on SDS-PAGE under reducing conditions.

≥ 90%, as determined by reducing SDS-PAGE.

Lyophilized powder.

Lyophilized from a 0.22 μm filtered solution of 20 mM Tris-HCl, 0.5 M NaCl, 6% trehalose, pH 8.0.
Note: For SPR assay, please replace the buffer. Primary amine components (e.g., Tris, imidazole) can affect protein-coupled chips.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.