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Mouse Anti-BLVRB Recombinant Antibody (CBYY-1655) (CBMAB-2004-YY)

This product is mouse antibody that recognizes BLVRB. The antibody CBYY-1655 can be used for immunoassay techniques such as: ELISA
See all BLVRB antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBYY-1655
Antibody Isotype
IgG2b
Application
ELISA

Basic Information

Immunogen
Recombinant Human BLVRB / biliverdin reductase B protein (Catalog#13151-H07E)
Specificity
Human
Antibody Isotype
IgG2b
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
biliverdin reductase B (flavin reductase (NADPH))
Introduction
The final step in heme metabolism in mammals is catalyzed by the cytosolic biliverdin reductase enzymes A and B (EC 1.3.1.24).
Entrez Gene ID
UniProt ID
Alternative Names
Biliverdin Reductase B; Short Chain Dehydrogenase/Reductase Family 43U, Member 1; Biliverdin-IX Beta-Reductase; Green Heme-Binding Protein; NADPH-Dependent Diaphorase; NADPH-Flavin Reductase; BVR-B; GHBP; FLR; FR; Biliverdin Reductase B (Flavin Reductase (NADPH));
Function
Broad specificity oxidoreductase that catalyzes the NADPH-dependent reduction of a variety of flavins, such as riboflavin, FAD or FMN, biliverdins, methemoglobin and PQQ (pyrroloquinoline quinone). Contributes to heme catabolism and metabolizes linear tetrapyrroles. Can also reduce the complexed Fe3+ iron to Fe2+ in the presence of FMN and NADPH. In the liver, converts biliverdin to bilirubin.
Biological Process
Heme catabolic process Source: UniProtKB
Cellular Location
Cytoplasm

Eisenmesser, E., Redzic, J. S., Duff, M. R., Blue, A., Pitts, T., & Agarwal, P. (2021). Modulating enzyme function via dynamic allostery within biliverdin reductase B. Frontiers in molecular biosciences, 8, 429.

Duff Jr, M. R., Redzic, J. S., Ryan, L. P., Paukovich, N., Zhao, R., Nix, J. C., ... & Eisenmesser, E. Z. (2020). Structure, dynamics and function of the evolutionarily changing biliverdin reductase B family. The Journal of Biochemistry, 168(2), 191-202.

Lok, C. N., Lai, Y. T., & Fung, Y. M. (2019). BILIVERDIN REDUCTASE B/FLAVIN REDUCTASE (BLVRB/FLR) EXHIBITS HEME-REGULATED, NADPH-DEPENDENT REDUCTASE ACTIVITY AND CONFERS CYTOPROTECTION IN DEVELOPING ERYTHROID CELLS. Experimental Hematology, 76, S76.

Nesbitt, N. M., Zheng, X., Li, Z., Manso, J. A., Yen, W. Y., Malone, L. E., ... & Bahou, W. F. (2018). In silico and crystallographic studies identify key structural features of biliverdin IXβ reductase inhibitors having nanomolar potency. Journal of Biological Chemistry, 293(15), 5431-5446.

Paukovich, N., Xue, M., Elder, J. R., Redzic, J. S., Blue, A., Pike, H., ... & Eisenmesser, E. Z. (2018). Biliverdin reductase B dynamics are coupled to coenzyme binding. Journal of molecular biology, 430(18), 3234-3250.

Matic, L. P., Jesus Iglesias, M., Vesterlund, M., Lengquist, M., Hong, M. G., Saieed, S., ... & Hedin, U. (2018). Novel multiomics profiling of human carotid atherosclerotic plaques and plasma reveals biliverdin reductase B as a marker of intraplaque hemorrhage. JACC: Basic to Translational Science, 3(4), 464-480.

Chu, W. T., Nesbitt, N. M., Gnatenko, D. V., Li, Z., Zhang, B., Seeliger, M. A., ... & Wang, J. (2017). Enzymatic activity and thermodynamic stability of biliverdin IXβ reductase are maintained by an active site serine. Chemistry (Weinheim an der Bergstrasse, Germany), 23(8), 1891.

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For research use only. Not intended for any clinical use.

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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