|Other Names||Flavin reductase (NADPH), FR, Biliverdin reductase B, BVR-B, Biliverdin-IX beta-reductase, Green heme-binding protein, GHBP, NADPH-dependent diaphorase, NADPH-flavin reductase, FLR, BLVRB, FLR|
|Target/Specificity||The synthetic peptide sequence is selected from aa 134-146 of HUMAN BLVRB|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Broad specificity oxidoreductase that catalyzes the NADPH-dependent reduction of a variety of flavins, such as riboflavin, FAD or FMN, biliverdins, methemoglobin and PQQ (pyrroloquinoline quinone). Contributes to heme catabolism and metabolizes linear tetrapyrroles. Can also reduce the complexed Fe(3+) iron to Fe(2+) in the presence of FMN and NADPH. In the liver, converts biliverdin to bilirubin.|
|Tissue Location||Predominantly expressed in liver and erythrocytes. At lower levels in heart, lung, adrenal gland and cerebrum.|
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Provided below are standard protocols that you may find useful for product applications.
The final step in heme metabolism in mammals is catalyzed by the cytosolic biliverdin reductase enzymes A and B (EC 22.214.171.124).
Persson, B., et al. Chem. Biol. Interact. 178 (1-3), 94-98 (2009) :
Smith, L.J., et al. Biochem. J. 411(3):475-484(2008)
Otterbein, L.E., et al. Trends Immunol. 24(8):449-455(2003)
Wang, J., et al. J. Biol. Chem. 278(22):20069-20076(2003)
Pereira, P.J., et al. Nat. Struct. Biol. 8(3):215-220(2001)
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