Heme Oxygenase 1, Rat (HMOX1) Recombinant Protein

HMOX1: 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 1 activity is highly inducible by its substrate heme and by various non-heme substances such as heavy metals, bromobenzene, endotoxin, oxidizing agents and UVA. Expressed at higher levels in renal cancer tissue than in normal tissue. Belongs to the heme oxygenase family.

Protein type: Cofactor and Vitamin Metabolism - porphyrin and chlorophyll; EC 1.14.99.3; Oxidoreductase

Cellular Component: endoplasmic reticulum membrane; endoplasmic reticulum; perinuclear region of cytoplasm; plasma membrane; nucleolus; caveola; cytosol; nucleus

Molecular Function: protein binding; signal transducer activity; protein homodimerization activity; enzyme binding; metal ion binding; phospholipase D activity; heme binding; oxidoreductase activity; heme oxygenase (decyclizing) activity

Biological Process: response to nicotine; cell death; negative regulation of smooth muscle cell proliferation; negative regulation of mast cell degranulation; positive regulation of smooth muscle cell proliferation; heme metabolic process; erythrocyte homeostasis; negative regulation of cell proliferation; regulation of transcription factor activity; heme catabolic process; small GTPase mediated signal transduction; regulation of blood pressure; phospholipid metabolic process; negative regulation of mast cell cytokine production; angiogenesis; negative regulation of neuron apoptosis; regulation of transcription from RNA polymerase II promoter in response to oxidative stress; healing during inflammatory response; protein homooligomerization; positive regulation of I-kappaB kinase/NF-kappaB cascade; negative regulation of transcription factor activity; heme oxidation; cellular response to nutrient; negative regulation of DNA binding; iron ion homeostasis; positive regulation of angiogenesis; DNA damage response, signal transduction resulting in induction of apoptosis; response to hydrogen peroxide; response to estrogen stimulus; response to hypoxia; response to oxidative stress