Protein name:
Heme oxygenase 2 (HO-2) ;
Alternative:
Organism:
Human (Homo sapiens).
General Annotation
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.
Subcellular Location:
Microsome
Endoplasmic reticulum
Protein Attributes:
50:
MSAEVETSEG | VDESEKKNSG | ALEKENQMRM | ADLSELLKEG | TKEAHDRAEN |
100:
TQFVKDFLKG | NIKKELFKLA | TTALYFTYSA | LEEEMERNKD | HPAFAPLYFP |
150:
MELHRKEALT | KDMEYFFGEN | WEEQVQCPKA | AQKYVERIHY | IGQNEPELLV |
200:
AHAYTRYMGD | LSGGQVLKKV | AQRALKLPST | GEGTQFYLFE | NVDNAQQFKQ |
250:
LYRARMNALD | LNMKTKERIV | EEANKAFEYN | MQIFNELDQA | GSTLARETLE |
300:
DGFPVHDGKG | DMRKCPFYAA | EQDKGALEGS | SCPFRTAMAV | LRKPSLQFIL |
Vaild Sequence:
Related Databases
Uniprot:
ELISA Kit
CLIA Kit
Polyclonal Antibody
Monoclonal Antibody
Protein
FOR
Human
Rat
Mouse
Rabbit
Polyclonal Antibody for Human HO-2
Polyclonal Antibody for Human HO-2
Polyclonal Antibody for Human HO-2
Polyclonal Antibody for Human HO-2
Monoclonal Antibody for Human HO-2
Monoclonal Antibody for Human HO-2
Monoclonal Antibody for Human HO-2
Monoclonal Antibody for Human HO-2
R&D Technical Data
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Precision
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Recovery
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Linearity
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[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
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