Recombinant Human Heme Oxygenase 1/HO-1 is produced with our E. coli expression system. The target protein is expressed with sequence (Met1-Thr261) of Human HO-1.
Pureté
> 95 % as determined by reducing SDS-PAGE.
Stérilité
0.2 μm filtered
niveau d'endotoxine
Less than 0.1 ng/μg (1 IEU/μg) as determined by LAL test
HMOX1
Origine: Humain
Hôte: Escherichia coli (E. coli)
Recombinant
> 95 % as determined by reducing SDS-PAGE.
Restrictions
For Research Use only
Format
Liquid
Reconstitution
It is not recommended to reconstitute to a concentration less than 100 μg/mL. Dissolve the lyophilized protein in ddH2O. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Buffer
Supplied as a 0.2 μm filtered solution of 20 mM PB, 150 mM NaCl, 1 mM EDTA, pH 7.4.
Conseil sur la manipulation
Always centrifuge tubes before opening. Do not mix by vortex or pipetting.
Stock
-80 °C
Stockage commentaire
Store at < -20°C, stable for 6 months after receipt. Please minimize freeze-thaw cycles.
Heme Oxygenase 1 (HO-1) is an enzyme in endoplasmic reticulum that belongs to the heme oxygenase family. HO-1 cleaves the heme ring at the alpha methene bridge to form Biliverdin. Biliverdin is subsequently converted to Bilirubin by Biliverdin reductase. In physiological state, the highest activity of HO-1 is found in the spleen, where senescent erythrocytes are sequestrated and destroyed. HO-1 activity is highly inducible by its substrate heme and by various non-heme substances such as heavy metals, bromobenzene, endotoxin, oxidizing agents and UVA. HO-1 is involved in the regulation of cardiovascular function and response to a variety of stressors. Defects in HO-1 are the cause of Heme Oxygenase 1 deficiency, resulting in marked erythrocyte fragmentation and intravascular hemolysis, coagulation abnormalities, endothelial damage, and iron deposition in renal and hepatic tissues. Alternative Names: Heme Oxygenase 1, HO-1, HMOX1, HO, HO1