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Source Escherichia coli
Amino Acid Sequence
Sequence MSAEVETSEG 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
Amino acids 1 to 264 Specifications
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 > 90
% SDS-PAGE. ab93468 is purified using conventional chromatography techniques.
Concentration information loading... Preparation and Storage
Stability and Storage
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
Constituents: 10% Glycerol, 20mM Tris, 1mM DTT, pH 8.0
Heme oxygenase (decycling) 2
Heme oxygenase (decyclizing) 2
Heme oxygenase 2
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. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter.
Sequence similarities Belongs to the heme oxygenase family. Contains 2 HRM (heme regulatory motif) repeats.
Cellular localization Microsome. Endoplasmic reticulum.
Information by UniProt
Recombinant Human Heme oxygenase 2 protein images
References for Recombinant Human Heme oxygenase 2 protein (ab93468)
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"