protein

BLVRB Protein, Human (His)

HY-P76172

5 μg;10 μg;50 μg

60;105;290 USD

BLVRB Protein, Human (His)

proteins

E. coli

5 μg;10 μg;50 μg

60;105;290 USD

The BLVRB protein is a broad-specificity oxidoreductase that catalyzes the NADPH-dependent reduction of a variety of substrates, including flavin, biliverdin, methemoglobin, and PQQ. It is essential in heme catabolism, metabolizing linear tetrapyrrole and reducing complexed Fe(3+) iron to Fe(2+) in the presence of FMN and NADPH. BLVRB Protein, Human (His) is the recombinant human-derived BLVRB protein, expressed by E. coli , with N-His labeled tag. The total length of BLVRB Protein, Human (His) is 205 a.a., with molecular weight of ~25 KDa.

Human

BLVRB Protein is a broad-specificity oxidoreductase with the ability to catalyze the NADPH-dependent reduction of various flavins, including riboflavin, FAD or FMN, as well as biliverdins, methemoglobin, and PQQ (pyrroloquinoline quinone). This enzyme plays a crucial role in heme catabolism, metabolizing linear tetrapyrroles. Additionally, it can reduce complexed Fe(3+) iron to Fe(2+) when FMN and NADPH are present. In the liver, BLVRB Protein serves a significant function by converting biliverdin to bilirubin, contributing to essential metabolic processes and maintaining redox balance.

Flavin reductase (NADPH); Biliverdin reductase B; FR; BVR-B; Green heme-binding protein (GHBP); FLR

Greater than 95% as determined by reducing SDS-PAGE

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4, 10% Glycerol.

Room temperature in continental US; may vary elsewhere.