Thioredoxin/TXN Protein, Human (Solution)

Thioredoxin/TXN protein participates in multiple redox reactions, utilizing its active center dithiol 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/TXN Protein, Human (Solution) is the recombinant human-derived Thioredoxin/TXN protein, expressed by E. coli , with tag free.

Thioredoxin/TXN Protein actively engages in diverse redox reactions, employing the reversible oxidation of its active center dithiol to form a disulfide bond, and catalyzes crucial dithiol-disulfide exchange reactions. Beyond its classical redox functions, Thioredoxin plays a pivotal role in the reversible S-nitrosylation of cysteine residues within target proteins, contributing to the cellular response to intracellular nitric oxide. Notably, it exerts regulatory control over caspase-3 activity by nitrosylating the active site cysteine of CASP3 in response to nitric oxide. Moreover, Thioredoxin demonstrates its influence on the FOS/JUN AP-1 DNA-binding activity in ionizing radiation cells, modulating AP-1 transcriptional activity through its oxidation/reduction status. Additionally, Thioredoxin is implicated in the augmentation of interleukin-2 receptor TAC (IL2R/P55) expression, highlighting its multifaceted role in cellular processes beyond redox regulation.

Human

E. coli

Tag Free

P10599 (M1-V105)

7295  [NCBI]

Full Length

MVKQIESKTAFQEALDAAGDKLVVVDFSATWCGPCKMIKPFFHSLSEKYSNVIFLEVDVDDCQDVASECEVKCMPTFQFFKKGQKVGEFSGANKEKLEATINELV

Approximately 14 kDa, based on SDS-PAGE under reducing conditions.

≥ 95%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.