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B3687

Sigma-Aldrich

Biliverdin Reductase A human

recombinant, expressed in E. coli, ≥90% (SDS-PAGE), buffered aqueous solution

Synonym(s):

BLVRA, BVRA, Bilirubin: NAD(P)+ oxidoreductase

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

recombinant

expressed in E. coli

Quality Level

Assay

≥90% (SDS-PAGE)

form

buffered aqueous solution

specific activity

≥700 units/mg protein

shipped in

dry ice

storage temp.

−20°C

Gene Information

human ... BLVRA(644)

General description

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.

Biochem/physiol Actions

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.

Unit Definition

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.

Physical form

Solution containing 20 mM potassium phosphate buffer, 10% glycerol, 0.2% Igepal CA630, 1 mM EDTA, and 0.1 mM DTT.

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
Peter E M Gibbs et al.
Frontiers in pharmacology, 6, 119-119 (2015-06-20)
Biliverdin reductase (BVR) is a multifunctional protein that is the primary source of the potent antioxidant, bilirubin. BVR regulates activities/functions in the insulin/IGF-1/IRK/PI3K/MAPK pathways. Activation of certain kinases in these pathways is/are hallmark(s) of cancerous cells. The protein is 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
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
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

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