Analytical Data
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Gene name
BLVRA
- Application
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Alternative Names
BLVRA；BLVR；BVR；Biliverdin reductase A
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P53004
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Expression Region
1-296aa
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AA Sequence
MNAEPERKFGVVVVGVGRAGSVRMRDLRNPHPSSAFLNLIGFVSRRELGSIDGVQQISLEDALSSQEVEVAYICSESSSHEDYIRQFLNAGKHVLVEYPMTLSLAAAQELWELAEQKGKVLHEEHVELLMEEFAFLKKEVVGKDLLKGSLLFTAGPLEEERFGFPAFSGISRLTWLVSLFGELSLVSATLEERKEDQYMKMTVCLETEKKSPLSWIEEKGPGLKRNRYLSFHFKSGSLENVPNVGVNKNIFLKDQNIFVQKLLGQFSEKELAAEKKRILHCLGLAEEIQKYCCSRK
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Molecular Weight
60.2kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
BLVRA, or Biliverdin Reductase A, is an essential enzyme in the heme catabolic pathway, responsible for the conversion of biliverdin to bilirubin. This process is crucial for maintaining cellular homeostasis and protecting against oxidative stress. Recent studies have highlighted the role of BLVRA in various physiological and pathological conditions, including its involvement in inflammation, neurodegenerative diseases, and cancer. The enzyme's ability to modulate cellular responses to oxidative stress and its interactions with various signaling pathways have made it a focal point for research aimed at understanding its broader implications in health and disease. Additionally, BLVRA's potential as a therapeutic target has garnered interest, prompting the investigation of its recombinant protein form. This approach aims to unravel the enzyme’s functional mechanisms, explore its structural properties, and assess its utility in clinical applications. Understanding BLVRA’s structure and function could lead to innovative strategies for treating disorders linked to its dysregulation, positioning it as a promising candidate for future therapeutic developments.
