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Source Escherichia coli
Amino Acid Sequence
Sequence MERPQPHSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTRDGFKLV MASLYHIYVA LEEEIERNKE SPVFAPVYFP EELHRKAALE QDLAFWYGPR WQEVIPYTPA MQRYVKRLHE VGRTEPELLV AHAYTRYLGD LSGGQVLKKI AQKALDLPSS GEGLAFFTFP NIASATKFKQ LYRSRMNSLE MTPAVRQRVI EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA SNKVQDSAPV ETPRGKPPLN TRSQAPLEHH HHHH
Amino acids 1 to 266
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.
Purity > 95
Concentration information loading... Preparation and Storage
Stability and Storage
Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.
Constituents: 10% Glycerol, 50mM Sodium chloride, 20mM Tris HCl, 0.1mM PMSF, pH 8
Function 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.
Sequence similarities Belongs to the heme oxygenase family.
Cellular localization Microsome. Endoplasmic reticulum.
Information by UniProt
Recombinant Human Heme Oxygenase 1 protein images
References for Recombinant Human Heme Oxygenase 1 protein (ab86919)
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"