An 11-aa peptide sequence within the N-terminus of rat HO-3 (1) was synthesized, coupled to KLH. Heme oxygenase is the rate-limiting microsomal enzyme in the heme degradative pathway. Heme oxygenase catalyzes the NADPH, O2 and cytochrome P450 reductase dependent oxidation of heme to form equimolar biliverdin, carbon monoxide, a putative neurotransmitter, and iron. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. These products of the HO reaction have important physiological effects: carbon monoxide is a potent vasodilator, biliverdin and its product bilirubin are potent antioxidants, free iron increases oxidative stress and regulates the expression of many mRNAs (e.g., DCT-1, ferritin and transferrin receptor) by affecting the conformation of iron regulatory protein (IRP)-1 and its binding to iron regulatory elements (IREs) in the 5- or 3-UTRs of the mRNAs. To date, 3 forms of heme oxygenases (HO1-3) have been identified. A third enzyme, HO-3 (rat 290 aa ~ 33kD) has been cloned and characterized from rat brain. The HO-3 mRNA is found in the spleen, liver, thymus, prostate, heart, kidney, brain and testis. The predicted amino acid structure of HO-3 differs from both HO-1 and HO-2 but is closely related to HO-2 (~ 90% similarity). HO-3 sequence has two HRM known to be involved in heme binding. It is a poor heme catalyst. Therefore, HO-3 has a potential regulatory role in heme-dependent cellular processes.
Purity:
Highly purified
Form:
Supplied as a liquid in PBS, pH 7.2
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