Anti-Heme oxidase 2/HMOX2 Antibody Picoband® fluoro550 Vervoeging

Heme oxygenase 2 (HMOX2), also known as HO-2, is an enzyme that in humans is encoded by the HMOX2 gene. It is mapped to 16p13.3. HMOX2 belongs to the heme oxygenase family. Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter.

Atypical chemokine receptor 2; C-C chemokine receptor D6; Chemokine receptor CCR-10; Chemokine receptor CCR-9; Chemokine-binding protein 2; Chemokine-binding protein D6; ACKR2; CCBP2; CCR10; CMKBR9; D6

HMOX2

3163

P30519

Human

No cross-reactivity with other proteins.

E.coli-derived human Heme oxygenase 2/HMOX2 recombinant protein (Position: H45-A301) .

Found in endothelial cells lining afferent lymphatics in dermis and lymph nodes. Also found in lymph nodes subcapsular and medullary sinuses, tonsillar lymphatic sinuses and lymphatics in mucosa and submucosa of small and large intestine and appendix. Also found in some malignant vascular tumors. Expressed at high levels in Kaposi sarcoma-related pathologies. Expressed on apoptotic neutrophils (at protein level) . Expressed primarily in placenta and fetal liver, and found at very low levels in the lung and lymph node.

Flow Cytometry

Chemokines, Immunology, Innate Immunity

Immunogen affinity purified.

Liquid

Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines including CCL2, CCL3, CCL3L1, CCL4, CCL5, CCL7, CCL8, CCL11, CCL13, CCL17, CCL22, CCL23, CCL24, SCYA2/MCP-1, SCY3/MIP-1-alpha, SCYA5/RANTES and SCYA7/MCP-3. Upon active ligand stimulation, activates a beta-arrestin 1 (ARRB1) -dependent, G protein-independent signaling pathway that results in the phosphorylation of the actin-binding protein cofilin (CFL1) through a RAC1-PAK1-LIMK1 signaling pathway. Activation of this pathway results in up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. By scavenging chemokines in tissues, on the surfaces of lymphatic vessels, and in placenta, plays an essential role in the resolution (termination) of the inflammatory response and in the regulation of adaptive immune responses. Plays a major role in the immune silencing of macrophages during the resolution of inflammation. Acts as a regulator of inflammatory leukocyte interactions with lymphatic endothelial cells (LECs) and is required for immature/mature dendritic cells discrimination by LECs.

1. McCoubrey WK Jr, Ewing JF, Maines MD (Jun 1992) . Human heme oxygenase-2: characterization and expression of a full-length cDNA and evidence suggesting that the two HO-2 transcripts may differ by choice of polyadenylation signal. Arch Biochem Biophys 295 (1) : 13–20. 2. Entrez Gene: HMOX2 heme oxygenase (decycling) 2

At -20 ̊C for one year from date of receipt. Avoid repeated freezing and thawing. Protect from light.

48608 MW

6

Atypical chemokine receptor 2

Cell membrane. Multi-pass membrane protein. Early endosome. Recycling endosome

Serine protease HTRA3

Rabbit IgG

Each vial contains 50% glycerol, 0.9% NaCl, 0.2% Na2HPO4, 0.02% NaN3.