ido Protein, Bacillus thuringiensis (FLAG, His)

IDO Protein, an enzyme, is involved in the conversion of tryptophan to kynurenine. Dysregulation of IDO Protein has been associated with immune suppression and tumor development. Targeting IDO Protein may present potential therapeutic approaches in cancer by modulating tryptophan metabolism, restoring immune responses, and inhibiting tumor growth. ido Protein, Bacillus thuringiensis (FLAG, His) is the recombinant ido protein, expressed by E. coli , with N-6*His, N-Flag labeled tag. The total length of ido Protein, Bacillus thuringiensis (FLAG, His) is 240 a.a., .

The ido protein emerges as a versatile catalyst, driving the hydroxylation of L-isoleucine to generate (4S)-4-hydroxy-L-isoleucine, a phenomenon documented across various studies. Beyond its role in L-isoleucine hydroxylation, ido showcases its enzymatic prowess by catalyzing the hydroxylation of L-leucine, L-norvaline, L-norleucine, and L-allo-isoleucine. Additionally, ido exhibits a broad substrate specificity, engaging in the sulfoxidation reactions of L-methionine, L-ethionine, S-methyl-L-cysteine, S-ethyl-L-cysteine, and S-allyl-L-cysteine. This enzymatic versatility positions the ido protein as a key player in diverse biochemical pathways, underscoring its impact on multiple metabolic processes.

Others

E. coli

N-6*His;N-Flag

E2GIN1 (M1-K240)

/

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

<1 EU/μg, determined by LAL method.