Thioredoxin/TRX Protein, Mouse

Thioredoxin/TRX proteins participate in multiple redox reactions, utilizing their reactive dithiol centers for reversible oxidation and disulfide bond formation. It catalyzes important dithiol-disulfide exchange and plays a key role in S-nitrosylation of cysteine residues in response to intracellular nitric oxide. Thioredoxin/TRX Protein, Mouse is the recombinant mouse-derived Thioredoxin/TRX protein, expressed by E. coli , with tag free. The total length of Thioredoxin/TRX Protein, Mouse is 105 a.a., with molecular weight of ~15 kDa.

Thioredoxin/TRX Protein is actively involved in diverse redox reactions, utilizing its active center dithiol to undergo reversible oxidation and disulfide formation, thereby catalyzing essential dithiol-disulfide exchange reactions. Beyond its classical redox functions, Thioredoxin plays a crucial role in the reversible S-nitrosylation of cysteine residues within target proteins, contributing to the cellular response to intracellular nitric oxide. Notably, it nitrosylates the active site cysteine of CASP3 in response to nitric oxide, effectively inhibiting caspase-3 activity. Moreover, Thioredoxin demonstrates regulatory influence over the FOS/JUN AP-1 DNA binding activity in ionizing radiation cells, modulating AP-1 transcriptional activity through its redox state. Additionally, Thioredoxin is implicated in the augmentation of interleukin-2 receptor TAC (IL2R/P55) expression, underscoring its multifaceted role in cellular processes beyond redox regulation.

Mouse

E. coli

Tag Free

P10639 (M1-A105)

22166  [NCBI]

Approximately 15 kDa

Greater than 95% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.