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Introduction | HMOX2 cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently transferred to bilirubin by biliverdin reductase. Under physiological conditions, the activity of HMOX2 is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. HMOX2 participates in the production of carbon monoxide in the brain where it operates as a neurotransmitter. HMOX2 is an essential enzyme in heme catabolism and is involved in cellular response to oxidative stress. |
Synonyms | EC 1.14.99.3, HO2, Heme oxygenase 2, HO-2, HMOX2. |
Source | Escherichia Coli. |
Physical Appearance | Sterile filtered colorless solution. |
Formulation | HMOX2 solution containing 20mM Tris pH-8, 1mM DTT and 10% glycerol. |
Stability | HMOX2 Human Recombinant althoµgh stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles. |
Amino Acid Sequence | SAEVETSEG VDESEKKNSG ALEKENQMRM ADLSELLKEG TKEAHDRAEN TQFVKDFLKG NIKKELFKLA TTALYFTYSA LEEEMERNKD HPAFAPLYFP MELHRKEALT KDMEYFFGEN WEEQVQCPKA AQKYVERIHY IGQNEPELLV AHAYTRYMGD LSGGQVLKKV AQRALKLPST GEGTQFYLFE NVDNAQQFKQ LYRARMNALD LNMKTKERIV EEANKAFEYN MQI |
Purity | Greater than 90% as determined by SDS-PAGE. |
Usage | NeoScientific's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drµgs, agricultural or pesticidal products, food additives or household chemicals. |
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