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BLVRB Protein, Human, Recombinant (His Tag)

Product Specifications

Background

Biliverdin reductase (hBVR) is a serine/threonine kinase that catalyzes reduction of the heme oxygenase (HO) activity product, biliverdin, to bilirubin. BVR consists of an N-terminal dinucleotide-binding domain (Rossmann-fold) and a C-terminal domain that contains a six-stranded β-sheet that is flanked on one face by several α-helices. The C-terminal and N-terminal domains interact extensively, forming the active site cleft at their interface. Biliverdin reductase (BVR) catalyzes the last step in heme degradation by reducing the γ-methene bridge of the open tetrapyrrole, biliverdin IXα, to bilirubin with the concomitant oxidation of a β-nicotinamide adenine dinucleotide (NADH) or β-nicotinamide adenine dinucleotide phosphate (NADPH) cofactor. It is now recognized that human BVR (hBVR) is a dual-specificity kinase (Ser / Thr and Tyr) upstream activator of the insulin/insulin growth factor-1 (IGF-1) and mitogen-activated protein kinase (MAPK) signaling pathways. Human BVR (hBVR) is essential for MAPK-extracellular signal-regulated kinase (ERK) 1/2 (MEK) -eukaryotic-like protein kinase (Elk) signaling and has been identified as the cytoplasm-nuclear heme transporter of ERK1/2 and hematin, the key components of stress-responsive gene expression.

Overview

A DNA sequence encoding the human BLVRB (P30043) (Ala 2-Gln 206) was expressed, with a polyhistide tag at the N-terminus.

Synonyms

BVRB Protein, Human; FLR Protein, Human; HEL-S-10 Protein, Human; SDR43U1 Protein, Human

Gene Name

Biliverdin reductase B

UniProt

P30043

Expression System

E. coli

Tag

N-His

Endotoxin

Please contact us for more information.

Purity

> 97 % as determined by SDS-PAGE.

Activity

At Leading Biology, the biological activity of a recombinant protein is routinely measured using a bioassay, e.g. chemotaxis or cell proliferation assay, enzyme assay, or a functional ELISA. When a recombinant protein is an enzyme, specific activity is derived from an enzymatic assay. Each enzyme is tested for potency by cleavage of a substrate. We are in the process of updating the biological activity data. If you have any questions regarding this update, please feel free to contact our technical support team.

Form

Lyophilized

Buffer

Lyophilized from sterile PBS, 0.02% Brij35, 10% glycerol, pH 7.5 Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.

Function

Enzyme Proteins

Molecular Weight

The recombinant human BLVRB consisting of 216 amino acids and has a calculated molecular mass of 23.5 kDa. It migrates as a kDa band in SDS-PAGE under reducing conditions as predicted.

Storage Conditions

In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise. Stable for 1 year at -20°C or below from date of shipment. For maximum recovery of product, centrifuge the original vial after thawing and opening the cap. For long-term storage, aliquot and store at -20°C or below. Avoid repeated freeze-thaw cycles.

Symbol

BLVRB

Species

Human

Uniprot URL

https://www.uniprot.org/uniprot/P30043

AA Sequence

Ala2-Gln206

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