Anti-Heme Oxygenase-3 (HO-3)

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 290aa ~ 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. Applications: Suitable for use in ELISA. Western Blot, though not tested, may potentially be used as an application. Other applications not tested. Recommended Dilutions: ELISA: 1:10,000-1:100,000 using 50-100ng control peptide/well., Western Blot: 1-10ug/ml using ECL. , Optimal dilutions to be determined by the researcher. Recommended Control Peptide: H1847-97: Heme Oxygenase 3, Rat (HO-3) Control Peptide, Storage and Stability: May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.