Bacteria-Derived HO-1 Recombinant Protein from Innovative Research has been recombinantly produced in E.coli. The protein formulation is supplied as a 0.2 ?m filtered solution of 20mM PB, 150mM NaCl, 1mM EDTA, pH 7.4. with a purity of > 95 % as determined by reducing SDS-PAGE..

More Details:

• Species: Human
• Target: HO-1
• Purity: > 95 % as determined by reducing SDS-PAGE..< 1.0 EU per ug as determined by the LAL method.
• Source: E.coli
• Storage Conditions: Store at < -20°C, stable for 6 months. 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.

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This material is sold for in-vitro use only for manufacturing and research. This material is not suitable for human or animal use. While we make every effort to ensure the safety of our products, we recommend handling any biological materials with standard precautions as if capable of spreading infectious disease. The statements herin are offered for informational purposes only to be used solely for your consideration, investigation, and verification.

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