Analytical Data
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Gene name
BLVRB
- Application
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Alternative Names
FLR; SDR43U1; Flavin Reductase,NADPH; Short Chain Dehydrogenase/Reductase Family 43U,Member 1; Biliverdin-IX beta-reductase; Green heme-binding protein
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P30043
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Expression Region
Ala2~Gln206
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Molecular Weight
26kDa
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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
The BLVRB protein, also known as biliverdin reductase B, plays a critical role in the cellular metabolism of heme, converting biliverdin to bilirubin, which is an important antioxidant. Understanding the BLVRB protein's structure and function is vital in the context of various biological processes, including oxidative stress response and cellular signaling pathways. Dysregulation of BLVRB has been implicated in several diseases, such as cancer, neurodegenerative conditions, and cardiovascular disorders, making it a potential therapeutic target. Researchers have focused on elucidating the protein's mechanism of action, its interactions with other cellular molecules, and the potential for developing BLVRB inhibitors or activators. Recent advances in structural biology techniques, such as X-ray crystallography and cryo-electron microscopy, have provided deeper insights into the protein's conformational dynamics and regulatory mechanisms. Furthermore, the exploration of BLVRB's role in metabolism and its therapeutic implications underscores its importance in biomedical research, as it opens new avenues for the development of targeted therapies aimed at modulating its activity for improved health outcomes. As the understanding of BLVRB continues to evolve, it holds promise for advancing treatments for diseases where oxidative stress plays a pivotal role.
