B3687
Biliverdin Reductase A human
recombinant, expressed in E. coli, ≥90% (SDS-PAGE), buffered aqueous solution
Synonyme(s) :
BLVRA, BVRA, Bilirubin: NAD(P)+ oxidoreductase
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About This Item
Code UNSPSC :
12352200
Nomenclature NACRES :
NA.32
Produits recommandés
Produit recombinant
expressed in E. coli
Niveau de qualité
Pureté
≥90% (SDS-PAGE)
Forme
buffered aqueous solution
Activité spécifique
≥700 units/mg protein
Conditions d'expédition
dry ice
Température de stockage
−20°C
Informations sur le gène
human ... BLVRA(644)
Description générale
Research area: IMMUNO AND CKS. Biliverdinreductase A (BVRA) is an isozyme of the biliverdin reductase. It is a cellsurface membrane receptor. BVRA consists of two major regions, theregulatory/DNA interaction domain and catalytic domain.
Application
Biliverdin Reductase Ahuman has been used as a component of the incubation medium to evaluate theactivity of hemeoxygenase 1. It has also been used as a standard todetermine the age of the bleed from haemorrhagic lesion.
Actions biochimiques/physiologiques
Biliverdin reductase catalyzes the transformation of the blue-green pigment biliverdin IX to the yellow-orange bile pigment bilirubin IX by converting a double-bond between the second and third pyrrole ring into a single-bond. This enzyme has two distinct cofactor-dependent pH optima. In the acidic range of pH 6.0-6.7, NADH is utilized, whereas in the alkaline range of pH 8.5-8.7, NADPH is utilized. Biliverdin reductase is considered a major physiologic cytoprotectant. Biliverdin reductase suppresses experimental autoimmune encephalomyelitis in rats. Depletion of biliverdin reductase leads to accumulation of cellular oxidants and augmented cell death.Biliverdin reductase (BVR)modulates the functions of insulin via the insulin-like growth factor 1 (IGF-1)pathway. It shows dual specificity kinases where it phosphorylates tyrosineapart from serine and threonine. BVR acts as a biomarker in certain cancers.
Définition de l'unité
1 unit of biliverdin reductase will transform 1 nanomole of biliverdin to bilirubin per minute in an NADPH dependent reaction at pH 8.5 using 100 mM K-phosphate buffer at 37 °C.
Forme physique
Solution containing 20 mM potassium phosphate buffer, 10% glycerol, 0.2% Igepal CA630, 1 mM EDTA, and 0.1 mM DTT.
Code de la classe de stockage
12 - Non Combustible Liquids
Classe de danger pour l'eau (WGK)
WGK 2
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
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Kristin A Kirkby et al.
American journal of physiology. Renal physiology, 290(3), F563-F571 (2006-02-08)
Heme oxygenase 1 (HO-1) is induced in response to cellular stress and is responsible for converting the prooxidant heme molecule into equimolar quantities of biliverdin (BV), carbon monoxide (CO), and iron. BV is then converted to bilirubin (BR) by the
W Uerkvitz et al.
The Journal of biological chemistry, 256(1), 382-389 (1981-01-10)
Three periplasmic nucleoside monophosphate-splitting phosphatases from Salmonella typhimurium, 2':3'-cyclic nucleotide 2'-phosphodiesterase, nonspecific acid phosphatase I, and nonspecific acid phosphatase II, were separated by column chromatography. They are characterized with respect to their substrate specificities, Km values, pH optima, molecular weights
Elina M Sutinen et al.
Frontiers in cellular neuroscience, 8, 214-214 (2014-08-26)
Chronic inflammation and oxidative stress (OS) are present in Alzheimer's disease (AD) brains in addition to neuronal loss, Amyloid-β (Aβ) plaques and hyperphosphorylated tau-protein neurofibrillary tangles (NFTs). Previously we showed that levels of the pro-inflammatory cytokine, interleukin-18 (IL-18), are elevated
Ali Abbasi et al.
Nutrition and cancer, 73(10), 2003-2013 (2020-09-15)
To assess the effect of sequential treatment with Vitamin C (VC) and Quercetin (Q) on Nrf2-related oxidative stress in PC3 and DU145 cells, viability was measured by MTT assay. Intracellular ROS levels were determined, using 2'-7'-dichlorodihydrofluorescein diacetate fluorescent as a
Luke O'Brien et al.
Trends in endocrinology and metabolism: TEM, 26(4), 212-220 (2015-03-03)
The biliverdin reductase (BVR) isozymes BVRA and BVRB are cell surface membrane receptors with pleiotropic functions. This review compares, for the first time, the structural and functional differences between the isozymes. They reduce biliverdin, a byproduct of heme catabolism, to
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