Recombinant Human BLVRA Protein (C-6His)

Name: Recombinant Human BLVRA Protein (C-6His)
Brand: Beta LifeScience
SKU: BL-1622NP
Availability: InStock

BL-1622NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Biliverdin Reductase A is produced by our E.coli expression system and the target gene encoding Glu6-Ser294 is expressed with a 6His tag at the C-terminus.
Accession	P53004
Synonym	BLVRA;Biliverdin reductase A;BVR A;Biliverdin-IX alpha-reductase;BLVR;BVR
Gene Background	Human Biliverdin reductase A (BLVRA) is belonged to the Gfo/Idh/MocA family and Biliverdin reductase subfamily. BLVRA is an enzyme that in humans is encoded by the BLVRA gene. BLVRA plays an important role in reducing the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor. BLVRA acts on biliverdin by reducing its double-bond between the pyrrole rings into a single-bond. It accomplishes this using NADPH + H+ as an electron donor, forming bilirubin and NADP+ as products.
Molecular Mass	33.8 KDa
Apmol Mass	35-45 KDa, reducing conditions
Formulation	Supplied as a 0.2 μm filtered solution of 20mM Tris-HCl, 100mM NaCl, 50% Glycerol, pH 8.0.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution
Storage	Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping	The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

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

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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.