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Merck

B3687

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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50 μG

HUF 212,000.00

HUF 212,000.00


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About This Item

NACRES:
NA.32
UNSPSC Code:
12352200

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Product Name

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

recombinant

expressed in E. coli

assay

≥90% (SDS-PAGE)

form

buffered aqueous solution

specific activity

≥700 units/mg protein

shipped in

dry ice

storage temp.

−20°C

Quality Level

Gene Information

human ... BLVRA(644)

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SAB1411260SAB1405518SAB1403608
assay

≥90% (SDS-PAGE)

assay

-

assay

-

assay

-

Gene Information

human ... BLVRA(644)

Gene Information

human ... BLVRA(644)

Gene Information

human ... BLVRA(644)

Gene Information

human ... BLVRA(644)

specific activity

≥700 units/mg protein

specific activity

-

specific activity

-

specific activity

-

recombinant

expressed in E. coli

recombinant

-

recombinant

-

recombinant

-

form

buffered aqueous solution

form

buffered aqueous solution

form

buffered aqueous solution

form

buffered aqueous solution

shipped in

dry ice

shipped in

dry ice

shipped in

dry ice

shipped in

dry ice

Application

Biliverdin Reductase Ahuman has been used as a component of the incubation medium to evaluate theactivity of hemeoxygenase 1.[1] It has also been used as a standard todetermine the age of the bleed from haemorrhagic lesion.[2]

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.[3] 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.[4] Biliverdin reductase is considered a major physiologic cytoprotectant. Biliverdin reductase suppresses experimental autoimmune encephalomyelitis in rats.[5] Depletion of biliverdin reductase leads to accumulation of cellular oxidants and augmented cell death.[6]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.[7]

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.[8]

Other Notes

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

12 - Non Combustible Liquids

wgk

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


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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
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
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
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

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