BLVRB Antibody (C-term)
Purified Rabbit Polyclonal Antibody (Pab)
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Application
| WB |
|---|---|
| Primary Accession | P30043 |
| Other Accession | Q923D2, P52556 |
| Reactivity | Human, Mouse |
| Predicted | Bovine |
| Host | Rabbit |
| Clonality | polyclonal |
| Calculated MW | 22119 Da |
| Isotype | Rabbit IgG |
| Antigen Source | HUMAN |
| Gene ID | 645 |
|---|---|
| Antigen Region | 161-175 aa |
| Other Names | Flavin reductase (NADPH), FR, Biliverdin reductase B, BVR-B, Biliverdin-IX beta-reductase, Green heme-binding protein, GHBP, NADPH-dependent diaphorase, NADPH-flavin reductase, FLR, BLVRB, FLR |
| Dilution | WB~~1:1000 |
| Target/Specificity | This BLVRB antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 161-175 amino acids from the C-terminal region of human BLVRB. |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | BLVRB Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
For Research Use Only. Not For Use In Diagnostic Procedures.
| Name | BLVRB (HGNC:1063) |
|---|---|
| Function | Enzyme that can both act as a NAD(P)H-dependent reductase and a S-nitroso-CoA-dependent nitrosyltransferase (PubMed:10620517, PubMed:18241201, PubMed:27207795, PubMed:38056462, PubMed:7929092). Promotes fetal heme degradation during development (PubMed:10858451, PubMed:18241201, PubMed:7929092). Also expressed in adult tissues, where it acts as a regulator of hematopoiesis, intermediary metabolism (glutaminolysis, glycolysis, TCA cycle and pentose phosphate pathway) and insulin signaling (PubMed:27207795, PubMed:29500232, PubMed:38056462). Has a broad specificity oxidoreductase activity by catalyzing the NAD(P)H-dependent reduction of a variety of flavins, such as riboflavin, FAD or FMN, biliverdins, methemoglobin and PQQ (pyrroloquinoline quinone) (PubMed:10620517, PubMed:18241201, PubMed:7929092). Contributes to fetal heme catabolism by catalyzing reduction of biliverdin IXbeta into bilirubin IXbeta in the liver (PubMed:10858451, PubMed:18241201, PubMed:7929092). Biliverdin IXbeta, which constitutes the major heme catabolite in the fetus is not present in adult (PubMed:10858451, PubMed:18241201, PubMed:7929092). Does not reduce bilirubin IXalpha (PubMed:10858451, PubMed:18241201, PubMed:7929092). Can also reduce the complexed Fe(3+) iron to Fe(2+) in the presence of FMN and NADPH (PubMed:10620517). Acts as a protein nitrosyltransferase by catalyzing nitrosylation of cysteine residues of target proteins, such as HMOX2, INSR and IRS1 (PubMed:38056462). S- nitroso-CoA-dependent nitrosyltransferase activity is mediated via a 'ping-pong' mechanism: BLVRB first associates with both S-nitroso-CoA and protein substrate, nitric oxide group is then transferred from S- nitroso-CoA to Cys-109 and Cys-188 residues of BLVRB and from S- nitroso-BLVRB to the protein substrate (PubMed:38056462). Inhibits insulin signaling by mediating nitrosylation of INSR and IRS1, leading to their inhibition (PubMed:38056462). |
| Cellular Location | Cytoplasm |
| Tissue Location | Predominantly expressed in liver and erythrocytes (PubMed:7929092). At lower levels in heart, lung, adrenal gland and cerebrum (PubMed:7929092). Expressed in adult red blood cells (PubMed:29932944). |
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
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 Fe(3+) iron to Fe(2+) in the presence of FMN and NADPH. In the liver, converts biliverdin to bilirubin.
REFERENCES
Chikuba K.,et al.Biochem. Biophys. Res. Commun. 198:1170-1176(1994).
Komuro A.,et al.Biol. Pharm. Bull. 19:796-804(1996).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Grimwood J.,et al.Nature 428:529-535(2004).
Mural R.J.,et al.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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