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You are here:Home » Antibodies » Antibodies-Enzymes, Reductase » Anti -Biliverdin Reductase (BVR)

Anti -Biliverdin Reductase (BVR)


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Clone Host Grade Applications
Polyclonal Rabbit Purified B IP
Cleavage of heme b (Fe-protoporphyrin IX) at the alpha-methene carbon bridge to form the open tetrapyrrole, biliverdin IXa and carbon monoxide (CO) is catalyzed by heme oxygenase (HO) isozymes HO- 1 and HO-2 (heme hydrogen-donor: oxygen oxidoreductase; EC In mammalian species biliverdin reductase (BVR; bilirubin: NAD(P)+ oxidoreductase; EC converts the open tetrapyrrole to bilirubin. This pathway is the only efficient way of making bilirubin and hence deterring activation of oxygen by the heme molecule. The two isozymes of heme oxygen, one of which is referred to as HO-1, is a member of the heat shock protein family (Hsp32), and the second, or HO-2, is a constitutive form and is expressed at exceedingly high levels in the brain and testes. The end products of the heme degradation process have important physiological activities. CO is suspected of being a potential messenger in the brain and systemic organs wherein by interacting with the heme-dependent form of guanylate cyclase it stimulates cGMP-production. Bile pigments have been demonstrated to display potent antioxidant activity and have effective antiviral activity against HIV and herpes virus. BVR is unique among all enzymes characterized to date in having two pH optima (6.8 and 8.7), using a different cofactor at each pH range (NADH at pH 7.0 and NADPH at pH 8.7). The enzyme displays pI and molecular mass microheterogeneity which appear to be a result of post translational modifications. In rat the enzyme also shows a tissue specific developmental pattern. BVR is not a inactivated by heat shock and its preexisting message is not sequestered from translation subsequent to thermal stress. Furthermore, the microheterogeneity of the reductase
is preserved under thermal stress. BVR is expressed not only in cells and brain regions that already display HO-1 and HO-2, but also in regions and cell types that have the potential of inducing stress proteins. Rat cDNA for BVR has been isolated and characterized. The deduced protein has 3 cysteine residues (Cys73, Cys281, and Cys290) which are involved in cofactor and substrate binding. Human BVR is a substantially longer polypeptide than the rat enzyme (41-42kD vs. 33kD), but is also dual cofactor, dual pH dependent, requires free SH groups for activity and displays pI and molecular mass microheterogeneity. The human and rat BVR share some antigenic epitopes and show immunochemical cross reactivity (1-8).
Catalog #B1150-05
ApplicationsSuitable for use in Western Blotting, Immunoprecipitation. Other applications not tested.
Recommended DilutionWestern Blotting: 1:5000
Immunoprecipitation: 1:100
Optimal dilutions to be determined by the researcher.
Storage and StabilityMay be stored at 4°C for short-term only. For long-term storage, store at -20°C. Aliquots are stable for at least 12 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
Clone TypePolyclonal
FormSupplied as a liquid in PBS, 0.1mM PMSF, 50% glycerol.
PurityPurified by ammonium sulfate precipitation.
ImmunogenRecombinant rat Biliverdin Reductase expressed in E. coli.
SpecificityDetects an ~41-42kD protein (human) and ~33kD protein (rat), corresponding to the apparent molecular mass of Biliverdin Reductase on SDS-PAGE Western Blots.
Species reactivityRat, mouse, E. coli, guinea pig, hamster, sheep (weak).
Important NoteThis product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.

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