Heme oxygenase, Recombinant, Human, aa2-291, His-Tag (HO-2, HMOX2)

Heme oxygenase (HO) is the rate limiting enzyme in heme catabolism (1). It cleaves heme to biliverdin, carbon monoxide, and iron, biliverdin is subsequently converted by biliverdin reductase to bilirubin. The mechanism of HO is unique in that heme serves as both the substrate of the enzyme and as the prosthetic group for the activation of iron-bound O2. HO activity is highest in spleen where senescent erythrocytes are sequestered and destroyed. Two isoforms, HO-1 and HO-2, are expressed in most tissues. HO-1 is an inducible enzyme in response to heavy metals, oxidative stress, cytokines, and many drugs (2). HO-2 is constitutively expressed in the brain and testes. HO-1 is expressed mainly in spleen, liver, and kidney. In addition to its activity in the heme degradation pathway, erves as an oxygen sensor through its heme regulating motifs, which have the core sequence of Cys-Pro (3). Source: Recombinant protein corresponding to aa2-291 from human HO-2/HMOX2, fused to 6-his tag at C-terminal, expressed in E. coli. Molecular Weight: ~31 & 35kD, Endotoxin: <1.0EU/1ug (LAL method). 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.