protein

CDO1/Cysteine dioxygenase type 1 Protein, Human (His)

HY-P70066

10 μg;50 μg

57;160 USD

CDO1/Cysteine dioxygenase type 1 Protein, Human (His)

proteins

E. coli

10 μg;50 μg

57;160 USD

Cysteine dioxygenase (CDO1) plays a crucial role in cellular metabolism by catalyzing the oxidation of cysteine to cysteine sulfenic acid, a key step involving the addition of molecular dioxygen . This enzymatic process underlies cysteine catabolism and helps regulate sulfur amino acid metabolism. CDO1/Cysteine dioxygenase type 1 Protein, Human (His) is the recombinant human-derived CDO1/Cysteine dioxygenase type 1 protein, expressed by E. coli , with N-6*His labeled tag. The total length of CDO1/Cysteine dioxygenase type 1 Protein, Human (His) is 200 a.a., with molecular weight of 20-28 kDa.

Human

Cysteine dioxygenase type 1 (CDO1) is a crucial enzyme that catalyzes the oxidation of cysteine to cysteine sulfinic acid through the addition of molecular dioxygen. This enzymatic process represents a key step in the catabolism of cysteine, regulating the conversion of this amino acid to its sulfinic acid derivative. The activity of CDO1 is significant for maintaining cellular homeostasis and contributing to sulfur metabolism. By facilitating the oxidation of cysteine, CDO1 plays a pivotal role in regulating the levels of this amino acid and its downstream metabolites, influencing various physiological processes. This enzyme's involvement in cysteine catabolism underscores its importance in cellular sulfur metabolism and highlights its potential impact on redox balance and other metabolic pathways.

rHuCysteine dioxygenase type 1/CDO1, His; Cysteine Dioxygenase Type 1; Cysteine Dioxygenase Type I; CDO; CDO-I; CDO1

Greater than 95% as determined by reducing SDS-PAGE

Supplied as a 0.2 μm filtered solution of 20 mM Tris-HCl, 1 mM DTT, 10% Glycerol, pH 8.0.

Shipping with dry ice