Recombinant Human BVR protein is a Human Full Length protein, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
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Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
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Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IXalpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor (PubMed:10858451, PubMed:7929092, PubMed:8424666, PubMed:8631357). Does not reduce bilirubin IXbeta (PubMed:10858451). Uses the reactants NADH or NADPH depending on the pH; NADH is used at the acidic pH range (6-6.9) and NADPH at the alkaline range (8.5-8.7) (PubMed:7929092, PubMed:8424666, PubMed:8631357). NADPH, however, is the probable reactant in biological systems (PubMed:7929092).
BLVR, BVR, BLVRA, Biliverdin reductase A, BVR A, Biliverdin-IX alpha-reductase
Recombinant Human BVR protein is a Human Full Length protein, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 0.316% Tris HCl
ab87761 is purified using conventional chromatography techniques.
Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IXalpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor (PubMed:10858451, PubMed:7929092, PubMed:8424666, PubMed:8631357). Does not reduce bilirubin IXbeta (PubMed:10858451). Uses the reactants NADH or NADPH depending on the pH; NADH is used at the acidic pH range (6-6.9) and NADPH at the alkaline range (8.5-8.7) (PubMed:7929092, PubMed:8424666, PubMed:8631357). NADPH, however, is the probable reactant in biological systems (PubMed:7929092).
Belongs to the Gfo/Idh/MocA family. Biliverdin reductase subfamily.
Endotoxin Level: < 1.0 EU per 1 µg of protein (determined by LAL method).Protein previously labeled as Biliverdin Reductase.
The BVR protein known in full form as Biliverdin Reductase plays an essential mechanical role in the conversion of biliverdin to bilirubin. It exists as two main isoforms BVR-A and BVR-B with molecular masses approximately of 33 kDa. BVR is widely expressed in various tissues with higher levels found in liver kidney and spleen. As an enzyme its main function centers around the redox cycle between biliverdin and bilirubin providing an antioxidant defense mechanism.
BVR influences cell signaling and growth processes acting as a multifunctional enzyme beyond its primary reductive activity. It participates in the MAPK and PI3K/Akt signaling pathways acting both as a kinase and phosphatase which affects transcription factor regulation. BVR is also involved in heme metabolism working in conjunction with heme oxygenase to recycle heme a vital cellular molecule.
BVR significantly contributes to the antioxidative and anti-inflammatory pathways. It operates within the heme catabolic pathway and the MAPK signaling cascade linking to proteins like heme oxygenase-1 (HO-1) and the transcription factor Nrf2. These pathways support cell response to oxidative stress and regulate gene expression in response to environmental stressors.
BVR is associated with conditions such as jaundice and chronic inflammation-oriented diseases. Its interaction with proteins like heme oxygenase-1 (HO-1) elevates its importance in managing oxidative stress-related disorders. Disruption in BVR function or expression can influence bilirubin metabolism potentially leading to hyperbilirubinemia and contributing to inflammatory disease development through altered cell signaling.
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15% SDS-PAGE analysis of 3μg ab87761.
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