Recombinant Human HO-1/HMOX1 Protein (PKSH032529)
For research use only.
| Synonyms | HMOX1, HO, HO-1, HO1, Heme Oxygenase 1 |
| Species | Human |
| Expression Host | E.coli |
| Sequence | Met 1-Thr 261 |
| Accession | P09601 |
| Calculated Molecular Weight | 29.9 kDa |
| Observed Molecular Weight | 30 kDa |
| Tag | None |
| Bio-activity | Not validated for activity |
| Purity | > 95 % as determined by reducing SDS-PAGE. |
| Endotoxin | < 1.0 EU per μg of the protein as determined by the LAL method. |
| Storage | Store at < -20°C, stable for 6 months. Please minimize freeze-thaw cycles. |
| Shipping | This product is provided as liquid. It is shipped at frozen temperature with blue ice/gel packs. Upon receipt, store it immediately at < - 20°C. |
| Formulation | Supplied as a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, 1mM EDTA, pH 7.4. |
| Reconstitution | Not Applicable |
| Background | 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. |
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