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Full length protein
Amino Acid Sequence
MERPQLDSMSQDLSEALKEATKEVHIRAENSEFMRNFQKGQVSREGFKLV MASLYHIYTALEEEIERNKQNPVYAPLYFPEELHRRAALEQDMAFWYGPH WQEAIPYTPATQHYVKRLHEVGGTHPELLVAHAYTRYLGDLSGGQVLKKI AQKAMALPSSGEGLAFFTFPSIDNPTKFKQLYRARMNTLEMTPEVKHRVT EEAKTAFLLNIELFEELQALLTEEHKDQSPSQTEFLRQRPASLVQDTTSA ETPRGKSQISTSSSQTPLLRWVLTLSFLLATVAVGIYAM
1 to 289
Additional sequence information
Abpromise guarantee covers the use of
in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Stability and Storage
Shipped at 4°C. Store at -80°C.
Constituents: 0.003% EDTA, 0.1% Triton-X-100, 0.38% Potassium chloride, 0.24% Tris, 0.2% sodium cholate hydrate
Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed.
Belongs to the heme oxygenase family.
Microsome. Endoplasmic reticulum.
Information by UniProt
has not yet been referenced specifically in any publications.
Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"