A 26-aa peptide sequence near the middle of the Human HO-2 (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. HO-2 (mouse/rat 315 aa; human 316 aa; chromosome 16) is non-inducible form. Except for corticosterone, no other inducer of HO-2 has been identified to date. HO-2 has been localized to endothelial cells and adventitial nerves of blood vessels. It is also localized to neurons in autonomic ganglia, including the petrosal, superior cervical, and nodose ganglia, as well as ganglia in the myenteric plexus of the intestine. Low levels of Ho-2 are found in most tissues except spleen. At the amino acid level,HO-1 and HO-2 are 42% homologous. However, each isozyme is evolutionary highly conserved. The molecular weight of mammalian HO-1 is ~31-33kDa and HO-2 is ~36kDa.
仕様
Size：100ug
Source Antigen：Human synthetic peptide
Grade：Highly Purified
Purity：Highly purified
Form：Supplied as a liquid in PBS, pH 7.2
Specificity：Sequence is 100% conserved in mouse, rat, human HO-2
