Anti-Heme Oxygenase-1 Antibody

Reconstitute lyophilized antibody using ultrapure to a final concentration no less than 100 ug/mL. Reconstitution with PBS or Tris buffer is acceptable if required. Protein carrier, biocide or cryopreservative can be added as needed. Aliquot and store at -20C for longterm storage. Dilute immediately prior to use.

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.

Immunoblotting: use at 5-10ug/mL. A band of ~33kDa is detected. <br><br>Immunohistochemistry: use at 5-10ug/mL on human frozen or paraffin-embedded tissue. Antigen retrieval with 0.4ug/mL Proteinase K. <br><br>These are recommended concentrations. <br><br>Endusers should determine optimal concentrations for their applications.

Stock solution of 2mg/ml should be stored for one (1) year at -20°C in appropriate aliquots to avoid multiple freeze-thaw cycles or at 4°C for 6 months with the addition of 0.1% sodium azide. Diluted antibody should not be stored.

Heme-oxygenase is an enzyme that catalyzes heme catabolism to yield biliverdin, iron, and carbon monoxide (CO). There are three isoforms of heme-oxygenase: HO-1, HO-2, and HO-3. HO-1 and HO-2 have been identified as the two major isoforms in mammals. HO-1, also known as heat shock protein 32 (Hsp32) is induced by most oxidative stress inducers, cytokines, inflammatory agents, and heat shock. HO-1 deficiency appears to cause reduced stress defense, a pro-inflammatory tendency, susceptibility to atherosclerotic lesion formation, endothelial cell injury, and growth retardation. Therefore, up-regulation of HO-1 is one of the major defense mechanisms against oxidative stress.