Biliverdin Reductase A/BLVRA Protein, Human (N-His)

Biliverdin Reductase A/BLVRA catalyzes the reduction of biliverdin IX alpha to bilirubin, utilizing either NADH or NADPH as a cofactor. The pH-dependent preference involves NADH at acidic pH (6-6.9) and NADPH at alkaline pH (8.5-8.7), with NADPH being the predominant reactant in biological systems. This enzymatic activity plays a crucial role in heme catabolism, influencing physiological processes and cellular redox balance. Biliverdin Reductase A/BLVRA Protein, Human (N-His) is the recombinant human-derived Biliverdin Reductase A/BLVRA protein, expressed by E. coli , with N-6*His labeled tag. The total length of Biliverdin Reductase A/BLVRA Protein, Human (N-His) is 289 a.a., with molecular weight of ~40 kDa.

The Biliverdin Reductase A/BLVRA protein serves as a catalyst in the reduction of the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin, accompanied by the oxidation of a NADH or NADPH cofactor. The choice between NADH and NADPH as a cofactor is pH-dependent, with NADH being utilized in the acidic pH range (6-6.9) and NADPH at the alkaline range (8.5-8.7). In biological systems, however, NADPH is considered the probable and more prevalent reactant. This enzymatic activity highlights the pivotal role of BLVRA in the conversion of biliverdin to bilirubin, a critical step in heme catabolism with implications for various physiological processes and cellular redox balance.

Human

E. coli

N-6*His

P53004 (E6-S294)

644  [NCBI]

ERKFGVVVVGVGRAGSVRMRDLRNPHPSSAFLNLIGFVSRRELGSIDGVQQISLEDALSSQEVEVAYICSESSSHEDYIRQFLNAGKHVLVEYPMTLSLAAAQELWELAEQKGKVLHEEHVELLMEEFAFLKKEVVGKDLLKGSLLFTAGPLEEERFGFPAFSGISRLTWLVSLFGELSLVSATLEERKEDQYMKMTVCLETEKKSPLSWIEEKGPGLKRNRYLSFHFKSGSLENVPNVGVNKNIFLKDQNIFVQKLLGQFSEKELAAEKKRILHCLGLAEEIQKYCCS

Approximately 40 kDa

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

<1 EU/μg, determined by LAL method.