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The region for expressing recombinant Human HMOX1 contains amino acids 3-288. The theoretical molecular weight of the HMOX1 protein is 36.6 kDa. This HMOX1 protein is produced using e.coli expression system. The HMOX1 gene fragment has been modified by fusing the N-terminal 6xHis tag, providing convenience in detecting and purifying the recombinant HMOX1 protein during the following stages.Human heme oxygenase 1 (HMOX1) is a crucial enzyme that plays a central role in heme catabolism. It catalyzes the degradation of heme into biliverdin, carbon monoxide (CO), and ferrous iron. Biliverdin is subsequently converted into bilirubin, an antioxidant with anti-inflammatory properties. HMOX1 is induced by various stimuli, including oxidative stress, inflammation, and environmental factors. Its expression is regulated by the transcription factor NRF2, which binds to the antioxidant response element (ARE) in the HMOX1 promoter. The enzymatic products generated by HMOX1 have protective effects against oxidative stress and inflammation. Research on HMOX1 is extensive, exploring its implications in diverse areas such as cellular stress response, inflammation, immune regulation, and its potential therapeutic applications in conditions associated with oxidative damage.
The region for expressing recombinant Human HMOX1 contains amino acids 3-288. The theoretical molecular weight of the HMOX1 protein is 36.6 kDa. This HMOX1 protein is produced using e.coli expression system. The HMOX1 gene fragment has been modified by fusing the N-terminal 6xHis tag, providing convenience in detecting and purifying the recombinant HMOX1 protein during the following stages.Human heme oxygenase 1 (HMOX1) is a crucial enzyme that plays a central role in heme catabolism. It catalyzes the degradation of heme into biliverdin, carbon monoxide (CO), and ferrous iron. Biliverdin is subsequently converted into bilirubin, an antioxidant with anti-inflammatory properties. HMOX1 is induced by various stimuli, including oxidative stress, inflammation, and environmental factors. Its expression is regulated by the transcription factor NRF2, which binds to the antioxidant response element (ARE) in the HMOX1 promoter. The enzymatic products generated by HMOX1 have protective effects against oxidative stress and inflammation. Research on HMOX1 is extensive, exploring its implications in diverse areas such as cellular stress response, inflammation, immune regulation, and its potential therapeutic applications in conditions associated with oxidative damage.
| Cat.No | ACP04309 | Target Name | HMOX1 |
|---|---|---|---|
| Form | Liquid or Lyophilized powder | Expression System | E.coli |
| Expression Range | 3-288aa | Mol Weight | 36.6kDa |
| Protein Length | Partial | Purity | Greater than 90% as determined by SDS-PAGE. |
| Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | P09601 |
|---|
Uniprot Id
P09601
Target Species
Human
Target Name
HMOX1
Target Full Name
Heme oxygenase 1
Target 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. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis.
Target Involvement
Heme oxygenase 1 deficiency (HMOX1D)
Target Subcellular Location
Microsome. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side.
Target Protein Families
Heme oxygenase family
Target Tissue Specificity
Expressed at higher levels in renal cancer tissue than in normal tissue (at protein level).
Target Research Area
Cardiovascular
Target Synonyms
32 kD; bK286B10; D8Wsu38e; heat shock protein 32 kD; heat shock protein 32kD; Heat shock protein; Heme oxygenase (decycling) 1; Heme oxygenase 1; Hemox; HMOX 1; Hmox; Hmox1; HMOX1_HUMAN; HO 1; HO; HO-1; HO1 ; Hsp32
Target Background
Heme oxygenase, an essential enzyme in heme catabolism, cleaves heme to form biliverdin, which is subsequently converted to bilirubin by biliverdin reductase, and carbon monoxide, a putative neurotransmitter. Heme oxygenase activity is induced by its substrate heme and by various nonheme substances. Heme oxygenase occurs as 2 isozymes, an inducible heme oxygenase-1 and a constitutive heme oxygenase-2. HMOX1 and HMOX2 belong to the heme oxygenase family.
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