HMOX2, Human

(EC 1.14.99.3, HO2, Heme oxygenase 2, HO-2, HMOX2.)

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.

HMOX2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 264 amino acids (1-264 a.a.) and having a molecular mass of 30.5 kDa. HMOX2 is purified by proprietary chromatographic techniques.

Purity: Greater than 90% as determined by SDS-PAGE.

Source: Escherichia Coli.

Physical Appearance: Sterile filtered colorless solution.

Formulation: HMOX2 solution containing 20mM Tris pH-8, 1mM DTT and 10% glycerol.

HMOX2 General Information

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 MQIFNELDQA GSTLARETLE DGFPVHDGKG DMRK.

Storage:
HMOX2 Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

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