BLVRB Mouse

Biliverdin Reductase B Mouse Recombinant
Cat. No.
BT17345
Source
Escherichia Coli.
Synonyms

Flavin reductase (NADPH), FR, Biliverdin reductase B, BVR-B, Biliverdin-IX beta-reductase, NADPH-dependent diaphorase, NADPH-flavin reductase, FLR.

Appearance
Sterile filtered colorless solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

BLVRB Mouse Recombinant produced in E. coli is a single, non-glycosylated polypeptide chain containing 229 amino acids (1-206 a.a) and having a molecular mass of 24.6kDa.
BLVRB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction

Biliverdin reductase B (BLVRB), also known as Enzyme Commission number (EC) 1.3.1.24, facilitates the transfer of electrons from reduced pyridine nucleotides to various molecules including flavins, methylene blue, pyrroloquinoline quinone, riboflavin, and methemoglobin. This enzyme plays a crucial role in protecting cells from oxidative stress and regulating iron metabolism. BLVRB catalyzes the reduction of biliverdin to bilirubin in the liver by converting a double bond between the second and third pyrrole ring into a single bond. It plays a vital role in the heme catabolic pathway of human erythrocytes and most mammalian species. BLVRB is highly expressed in organs such as the kidney, spleen, liver, and brain, while it is found at lower levels in the thymus and minimally detected in the testis.

Description

Recombinant Mouse BLVRB, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 229 amino acids, with 206 amino acids (1-206 a.a) forming the BLVRB protein and a 23 amino acid His-tag fused at the N-terminus. The molecular weight of the recombinant protein is 24.6 kDa. Purification is achieved using proprietary chromatographic techniques.

Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation

The BLVRB protein is supplied in a solution at a concentration of 0.5 mg/ml. The buffer consists of 20mM Tris-HCl at a pH of 8.0 and contains 10% glycerol.

Stability
For short-term storage (up to 2-4 weeks), the protein solution should be stored at 4°C. For extended storage, it is recommended to freeze the solution at -20°C. To ensure stability during long-term storage, adding a carrier protein like HSA or BSA at a concentration of 0.1% is advisable. Repeated freezing and thawing of the protein solution should be avoided.
Purity
The purity of the BLVRB protein is greater than 95%, as determined by SDS-PAGE analysis.
Synonyms

Flavin reductase (NADPH), FR, Biliverdin reductase B, BVR-B, Biliverdin-IX beta-reductase, NADPH-dependent diaphorase, NADPH-flavin reductase, FLR.

Source
Escherichia Coli.
Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH MGSMTVKKIA IFGATGRTGL TTLAQAVQAG YEVTVLVRDS SRLPSEGPQP AHVVVGDVRQ AADVDKTVAG QEAVIVLLGT GNDLSPTTVM SEGTRNIVTA MKAHGVDKVV ACTSAFLLWD PTKVPPRLQD VTDDHIRMHK ILQESGLKYV AVMPPHIGDQ PLTGAYTVTL DGRGPSRVIS KHDLGHFMLR CLTTNEYDGH TTYPSHQYD.

Product Science Overview

Introduction

Biliverdin Reductase B (BLVRB) is an enzyme that plays a crucial role in the heme metabolism pathway. It is responsible for the reduction of biliverdin to bilirubin, a process that is essential for the clearance of heme in mammals . This enzyme is part of the biliverdin reductase family and is encoded by the BLVRB gene.

Classification

Biliverdin Reductase B belongs to the short-chain dehydrogenase/reductase (SDR) family. It is also known by other names such as flavin reductase (NADPH) and NAD(P)H dehydrogenase (quinone) 1 . The enzyme is highly conserved across different species, including humans, mice, and rats .

Biological Properties

BLVRB is a cytosolic enzyme that exhibits dual cofactor specificity, meaning it can utilize both NADH and NADPH as electron donors . This property is significant for its role in various cellular processes, including oxidative stress response and cellular redox homeostasis.

Functions

The primary function of BLVRB is to catalyze the conversion of biliverdin to bilirubin. This reaction is crucial for the detoxification of heme, which is released during the breakdown of hemoglobin in senescent or damaged red blood cells . Bilirubin, the end product of this reaction, is a potent antioxidant that protects cells from oxidative damage .

Modes of Action

BLVRB operates by binding to biliverdin and reducing it to bilirubin using NAD(P)H as a cofactor. The enzyme’s active site contains a conserved tyrosine residue that is essential for its catalytic activity . The reduction process involves the transfer of electrons from NAD(P)H to biliverdin, resulting in the formation of bilirubin .

Regulatory Mechanisms

The expression and activity of BLVRB are regulated at multiple levels, including transcriptional, post-transcriptional, and post-translational modifications. Various factors such as oxidative stress, hypoxia, and inflammatory signals can influence the expression of BLVRB . Additionally, the enzyme’s activity can be modulated by phosphorylation and other post-translational modifications .

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