Human Biliverdin Reductase B,BLVRB ELISA Kit
- Known as:
- Human Biliverdin Reductase B,BLVRB Enzyme-linked immunosorbent assay test Kit
- Catalog number:
- dl-blvrb-hu
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Wuxi donglin
- Gene target:
- Human Biliverdin Reductase BLVRB ELISA Kit
Related genes to: Human Biliverdin Reductase B,BLVRB ELISA Kit
- Gene:
- BLVRB NIH gene
- Name:
- biliverdin reductase B
- Previous symbol:
- FLR
- Synonyms:
- SDR43U1
- Chromosome:
- 19q13.2
- Locus Type:
- gene with protein product
- Date approved:
- 1995-04-13
- Date modifiied:
- 2016-10-05
Related products to: Human Biliverdin Reductase B,BLVRB ELISA Kit
Related articles to: Human Biliverdin Reductase B,BLVRB ELISA Kit
- Myelofibrosis (MF) splenomegaly reflects not only extramedullary hematopoiesis (EMH) but a compartmental organization of the splenic microenvironment into spatially distinct niches. Using Spatial whole transcriptome profiling on FFPE spleen tissue from three MF patients, we interrogated three anatomically defined compartments: Intravascular (IV), Perivascular (PV) and Red Pulp (RP). Differential expression was estimated through pairwise compartment contrasts with Benjamini-Hochberg false discovery rate correction (FDR < 0.05, |log2FC|≥1), and compartment "core signatures" were defined by directional concordance across the two contrasts relevant to each compartment. IV regions of interest (ROIs) showed an endothelial/adhesion and vascular stress program (e.g., PECAM1, VCAM1; antioxidant enzymes). PV ROIs were characterized by fibro-remodeling and immune-structured signals (COL1A1/COL3A1, LOXL1, MMP2/TIMP1; HLA‑DRA/CD74) including CXCL12, consistent with a PV niche coupling extracellular matrix remodeling to hematopoietic retention cues. RP ROIs captured an EMH-associated erythroid/heme program (ALAS2, FECH, BLVRB) with stress and inflammatory alarmins (S100A8/S100A9). Together, these findings support a compartmental "division of labor" in MF spleen, vascular interface activation, PV remodeling/chemokine niches, and RP EMH/redox stress, providing a spatial framework to interpret splenomegaly as structured niche dependencies and to prioritize candidate microenvironmental dependencies for follow‑up validation. - Source: PubMed
Publication date: 2026/08/03
Peroni EdoardoPizzi MarcoBasso MarcoAtanasio AlessandroCalistri ElisabettaGottardi MicheleRosato Antonio - Hepatitis B virus (HBV) e antigen (HBeAg) plays a critical role in inducing macrophage activation and subsequent immune tolerance, which facilitates viral immune escape. However, the underlying spatial 3D genomic and epigenetic mechanisms driving this macrophage dysfunction remain largely unknown. - Source: PubMed
Publication date: 2026/07/16
Liu TiantianXie XiaoyuMa ShujunCao HuilingWang WenwenYu ZhenFeng YueminQi JianniBian Hongjun - Biliverdin IXb reductase (BLVRB) is an NAD(P)H-dependent oxidoreductase that regulates hematopoiesis and cellular stress, although measurement and sequelae of cellular active site engagement remain undefined. Here, we report the development of a nanoBRET platform enabling real-time BLVRB target engagement. Structure-guided design and chemical syntheses of BODIPY-labeled pyrazolopyrimidinone inhibitors generate cell-permeable acceptor ligands retaining high-affinity binding to the BLVRB active site. and cellular nanoBRET assays demonstrate specific energy transfer and inform equilibrium binding affinities, target engagement, and residence time analyses for diverse panels of BLVRB inhibitors. NanoBRET demonstrates strong concordance with enzymatic inhibition and is validated by crystallographic structures confirming active site binding. Live-cell imaging using affinity ligands reveals predominant endoplasmic reticulum localization and transient suppression of the ER stress chaperone GRP78/BiP without eliciting a canonical unfolded protein response. These studies inform a redox-regulated mechanism whereby spatiotemporal BLVRB active site engagement functions as a stress sensitizer modulating ER proteostasis. - Source: PubMed
Publication date: 2026/07/27
Thekke Veedu Rahul RaghavanSheriff JawaadNesbitt Natasha MMarchenko NataliaPennacchia LisaGinex TizianaHearing PatrickKreitler Dale FBahou Wadie F - Red blood cells (RBCs) are transcriptionally silent yet dynamically remodel metabolism in response to oxygen tension. Using ultra-pure human RBCs, we generated the deepest contamination-free proteome to date (3,775 proteins) and mapped the oxygen-dependent interactome. These datasets reveal an oxygen-responsive metabolon centered on the Band 3 (SLC4A1) N-terminus. We identify biliverdin reductase B (BLVRB) as a previously unrecognized Band 3 interactor that dissociates under hypoxia, coincident with increased Band 3-deoxyhemoglobin contacts. This reversible assembly functions as an oxygen-sensitive switch coordinating redox and glycolytic remodeling. Humanized mice lacking Band 3 N-terminal segments exhibit impaired oxygen-dependent regulation of BLVRB binding to band 3, impaired hypoxic activation of glycolysis, reduced 2,3-bisphosphoglycerate synthesis, and diminished exercise tolerance, demonstrating physiological relevance. Population-scale cis-pQTLs for SLC4A1 and BLVRB suggest functions beyond canonical heme catabolism. Mechanistically, biochemical analyses in vitro suggest that hemoglobin β (HBB), Band 3, and BLVRB can undergo S-nitrosation and may participate in trans-nitrosation reactions with the glycolytic enzyme GAPDH, whose modification at C152 inhibits enzymatic activity in vitro. Collectively, these findings define a Band 3-BLVRB axis that integrates oxygen-dependent protein interactions with thiol-based redox chemistry, providing a framework for understanding how an anucleate cell achieves metabolic adaptability through reversible protein-protein interactions and post-translational modification. These findings suggest that perturbation of the Band 3-BLVRB axis may influence oxygen delivery and metabolic flexibility during hypoxic stress, with potential relevance to high-altitude adaptation, exercise physiology, and cardiopulmonary disease. - Source: PubMed
Publication date: 2026/06/01
Issaian Aaron VaheDzieciatkowska MonikaBevers ShaunSafari ZohrehHay Ariel MCendali Francesca IArgabright AmyRogers Stephen CSaviola Anthony JRedzic Jasmina SWartchow EricReisz Haines JulieKeele Gregory RHaiman Zachary BNemkov TravisStephenson DanielLisk ChristinaVallese FrancescaPalsson Bernhard OKing S BrucePage Grier PDoctor AllanHudson Krystalyn EHansen Kirk CIrwin David CMohandas NarlaZimring James CEisenmesser Elan ZD'Alessandro Angelo - This study aimed to characterize systemic molecular signatures in the serum of patients with age-related cataracts and explore specific variations through integrated proteomic and metabolomic profiling. - Source: PubMed
Publication date: 2026/01/12
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