Recombinant Human Biliverdin Reductase A (BLVRA) Protein (GST)

Name: Recombinant Human Biliverdin Reductase A (BLVRA) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-09216P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description	Recombinant Human Biliverdin Reductase A (BLVRA) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P53004
Target Symbol	BLVRA
Synonyms	BIEA_HUMAN; Biliverdin IX alpha reductase; Biliverdin reductase A; Biliverdin-IX alpha-reductase; BLVR A; BLVR; Blvra; BVR A; BVR; BVRA; Zinc metalloprotein
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MNAEPERKFGVVVVGVGRAGSVRMRDLRNPHPSSAFLNLIGFVSRRELGSIDGVQQISLEDALSSQEVEVAYICSESSSHEDYIRQFLNAGKHVLVEYPMTLSLAAAQELWELAEQKGKVLHEEHVELLMEEFAFLKKEVVGKDLLKGSLLFTAGPLEEERFGFPAFSGISRLTWLVSLFGELSLVSATLEERKEDQYMKMTVCLETEKKSPLSWIEEKGPGLKRNRYLSFHFKSGSLENVPNVGVNKNIFLKDQNIFVQKLLGQFSEKELAAEKKRILHCLGLAEEIQKYCCSRK
Expression Range	1-296aa
Protein Length	Full Length
Mol. Weight	60.2kDa
Research Area	Signal Transduction
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor.
Subcellular Location	Cytoplasm.
Protein Families	Gfo/Idh/MocA family, Biliverdin reductase subfamily
Database References	HGNC: 1062 OMIM: 109750 KEGG: hsa:644 STRING: 9606.ENSP00000265523 UniGene: Hs.488143
Associated Diseases	Hyperbiliverdinemia (HBLVD)
Tissue Specificity	Liver.

Gene Functions References

Genetic polymorphisms of the UGT1A1 promoter, specifically the T-3279G phenobarbital-responsive enhancer module and (TA)7 dinucleotide repeat, as well as the intron and coding region variants of the OATP2, HMOX1, and BLVRA genes, were significantly higher among the cases than the controls. PMID: 27943244
BLVRA mRNA levels in the liver as well as in peripheral blood leukocytes are significantly higher in hepatocellular carcinoma patients most likely as a feedback mechanism to control increased oxidative stress associated with HCC progression. PMID: 27740521
Data suggest that isoenzymes BVRA and BVRB play different roles in energy metabolism and in pathogenesis of abdominal obesity and hypertriglyceridemia. [REVIEW] PMID: 25726384
Interactions of HO-2 with CPR and BVR, were evaluated. PMID: 25196843
Activation of human biliverdin-IXalpha reductase by urea: generation of kinetically distinct forms during the unfolding pathway. PMID: 24060811
These findings suggest that hBVR significantly contributes to the modulation of hypoxia-induced chemoresistance of glioblastoma cells by adjusting their cellular redox status. PMID: 24113378
Increased biliverdin reductase expression is associated with multidrug resistance in leukemia. PMID: 24222129
Our results suggest that patients with chronic HCV infection significantly upregulate BLVRA expression in PBL. PMID: 23536765
The current study reports increased levels of both HO-1 and BVR-A in plasma from probable Alzheimer disease patients, as a result of the increased oxidative environment. PMID: 22776971
rs699512 (Thr3Ala), the only common non-synonymous SNP within BLVRA, reduced the risk of essential hypertension in Kazaks. PMID: 21721974
A significant increase of nitrated BVRA was demonstrated only in Alzheimer's disease and mild cognitive impairment hippocampi PMID: 21483094
A homozygous BLVRA inactivating mutation is associated with the appearance of green jaundice accompanying cholestasis episodes. PMID: 21278388
data support the notion that BLVRA contributes significantly to modulation of the aging process by adjusting the cellular oxidative status. PMID: 21099244
An up-regulation of the biliverdin reductase-A protein levels was found in the hippocampus of the subjects with Alzheimer disease and arguably its earliest form, mild cognitive impairment. PMID: 21241799
hBVR was detected in the nucleus at 1, 2, and 4 h after hypoxia (1% O(2)), at which times its kinase and reductase activities were increased. PMID: 20410444
These observations support direct and indirect antioxidant properties of BVR and bilirubin and an important role for BVR and bilirubin in HO-1 conferred protection of endothelial cells. PMID: 20430037
Primary spontaneous pneumothorax in smokers is associated with lung macrophage oxidative stress. The response to this condition involves HIF-1alpha-mediated induction of HO-1, BVR and H-ferritin. PMID: 20526373
hBVR is a regulator of the TNF-alpha-GPBP-collagen type IV signaling cascade PMID: 20177069
Bilirubin, acting as a cytoprotective antioxidant, is itself oxidized to biliverdin and then recycled by biliverdin reductase back to bilirubin. This redox cycle may constitute the principal physiologic function of bilirubin. PMID: 12456881
Biliverdin reductase is a novel regulator for induction of activating transcription factor-2 and heme oxygenase-1 PMID: 14988408
BVR advances the role of HO-1 in cytoprotection and affords cytoprotection independent of heme degradation PMID: 15741166
hBVR activation of PKC betaII underscores its potential function in propagation of signals relayed through PKCs PMID: 17227757
Results describe the activation of biliverdin-IXalpha reductase by inorganic phosphate and related anions. PMID: 17402939
These findings, together with observations that si-hBVR blocked activation of ERK and Elk1 by IGF1 and prevented formation of ternary complex between MEK/ERK/hBVR, define the critical role of hBVR in ERK signaling and nuclear functions of the kinase. PMID: 18463290
Case Report: A novel mutation in the biliverdin reductase-A gene combined with liver cirrhosis results in hyperbiliverdinaemia (green jaundice). PMID: 19580635
Limited role for the bilirubin-biliverdin redox amplification cycle in the cellular antioxidant protection by biliverdin reductase. PMID: 19690164

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.