Heme Oxygenase-2 Human Recombinant ( HMOX2 Human )

Data sheet

Formulation

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

Purity

Greater than 90% as determined by SDS-PAGE.

Inactivation

Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.69 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program o

Description

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.

Protein Background

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 erythr

Expression host

Escherichia Coli.

Synonyms

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

Reagent Appearance

Sterile filtered colorless solution.

Stability

HMOX2 Human Recombinant although 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