|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.|
email@example.com, and receive a free "I Love Antibodies" mug.
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 18.104.22.168).
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)
If you have any additional inquiries please email technical services at firstname.lastname@example.org.