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HO-2 is a cellular myristate-binding protein that negatively regulates both virus replication and host inflammatory responses.
Our results suggest that rs1051308 is associated with risk of developing Parkinson disease in Han Chinese, and further studies involving various ethnicities are needed to validate the association.
High HMOX2 expression is associated with bladder cancer.
The present study suggests a weak association between HMOX2 rs1051308 polymorphism and the risk to develop multiple sclerosis (MS) in Spanish Caucasian men and a trend towards association between the HMOX1 (show HMOX1 ELISA Kits) rs2071746A and MS risk.
HMOX2 contributes to high-altitude adaptation in Tibetans by functioning as a modifier in the regulation of hemoglobin metabolism.
The same mechanism of heme hydroxylation to alpha-meso-hydroxyheme is employed by both isoforms HO-1 (show HMOX1 ELISA Kits) and HO-2.
a weak association between HMOX2 rs1051308 polymorphisms and the risk to develop essential tremor in the Spanish population.
Taken together with EPR (show EREG ELISA Kits) measurements, which show the appearance of a new low-spin heme signal in reduced HO2, it appears that a cysteine residue(s) in the HRMs directly interacts with a second bound heme
HO-2 protein is expressed in the cytosols of skin cancer cells.
Interactions of HO-2 with CPR (show POR ELISA Kits) and BVR (show BLVRA ELISA Kits), were evaluated.
This study demonstrated that Deletion of the heme oxygenase-2 aggravates brain injury following stroma-free hemoglobin-induced
Data indicate that injury induced heme oxygenase 1 (HO-1 (show HMOX1 ELISA Kits)) expression in both heme oxygenase 2 (HO-2) knockout and wild type mice.
HO-2 shRNA and HO-2 overexpression plasmids were used to observe the effect of HO-2 in cerebral microvascular endothelial cells. mRNA and protein levels of TNF-alpha (show TNF ELISA Kits) and IL6 (show IL6 ELISA Kits) were increased and decreased, respectively, compared with control groups.
macrophage HO-2 is required for proper macrophage function but is insufficient to correct the impaired healing of the HO-2(-/-) cornea, suggesting that corneal epithelial expression of HO-2 is a key to resolution and repair in wound healing
These results demonstrate a sex-specific effect of HO-2 deficiency on the development of renovascular hypertension and its effects on the heart in response to the increase in blood pressure.
HO-2 critically contributes to the adequacy of arteriovenous fistula blood flow and function.
protein-protein interactions between HO-2 and adiponectin (show ADIPOQ ELISA Kits) highlight the role of HO-2 as a molecular chaperone (show HSP90AA1 ELISA Kits) for adiponectin (show ADIPOQ ELISA Kits) assembly, while HO-1 (show HMOX1 ELISA Kits) increases adiponectin (show ADIPOQ ELISA Kits) levels.
PFKFB4 (show PFKFB4 ELISA Kits) and HO-2 are expressed in a coordinated manner to maintain glucose homeostasis.
ells other than neutrophils contribute to the exaggerated inflammation and impaired wound healing seen in the HO-2 null cornea
deficiency in HO-2 alters both the kinetics of secondary damage and fine motor recovery after traumatic brain injuries.
Heme-oxygenase-2 immunoreactivity was found in neurons of myenteric ganglia and in nerve fibers in the circular and longitudinal muscle layers.
HO-2 is critical for protection of cerebrovascular endothelium against apoptotic changes induced by oxidative stress and cytokine-mediated inflammation.
Heme oxygenase, an essential enzyme in heme catabolism, cleaves heme to form biliverdin, which is subsequently converted to bilirubin by biliverdin reductase, and carbon monoxide, a putative neurotransmitter. Heme oxygenase activity is induced by its substrate heme and by various nonheme substances. Heme oxygenase occurs as 2 isozymes, an inducible heme oxygenase-1 and a constitutive heme oxygenase-2. HMOX1 and HMOX2 belong to the heme oxygenase family. Alternative splice variants encoding the same protein have been identified at this locus.
heme oxygenase (decyclizing) 2
, heme oxygenase (decycling) 2
, heme oxygenase 2
, Heme oxygenase 2
, heme oxygenase-2 non-reducing isoform
, heme oxygenase-2